User:Ashley Crotteau/Sandbox1 - Revision history

Ashley Crotteau at 15:39, 26 April 2019

Ashley Crotteau — Fri, 26 Apr 2019 15:39:54 GMT

←Older revision		Revision as of 15:39, 26 April 2019
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-	The most notable feature of the HKMT is the presence of the lysine access channel as the active site. The cofactor and <scene name='81/811707/~~Sam_structure~~/1'>peptide</scene> substrate are located on opposite sides of the SET domain but are connected through this narrow channel (Figure 2).<ref name="Xiao" /> This channel allows these two components to interact and complete the methyltransfer. The active site in general is considerably tyrosine rich. Residues Tyr245, His297, Ser268, Tyr305, Tyr335, and Tyr337 all help to shape the <scene name='81/811707/Stick_active_site/3'>active site</scene> and the channel.<ref name="Xiao" /> The cofactor involved, SAM, provides the methyl for methylation of the lysine on its sulfur atom.	+	The most notable feature of the HKMT is the presence of the lysine access channel as the active site. The cofactor and <scene name='81/811707/Peptide/1'>peptide</scene> substrate are located on opposite sides of the SET domain but are connected through this narrow channel (Figure 2).<ref name="Xiao" /> This channel allows these two components to interact and complete the methyltransfer. The active site in general is considerably tyrosine rich. Residues Tyr245, His297, Ser268, Tyr305, Tyr335, and Tyr337 all help to shape the <scene name='81/811707/Stick_active_site/3'>active site</scene> and the channel.<ref name="Xiao" /> The cofactor involved, SAM, provides the methyl for methylation of the lysine on its sulfur atom.

Ashley Crotteau at 23:13, 25 April 2019

Ashley Crotteau — Thu, 25 Apr 2019 23:13:03 GMT

←Older revision		Revision as of 23:13, 25 April 2019
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	The ΔSET7/9 consists of the [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain] along with the pre- and post-SET regions.<ref name="Schubert" /><ref name="Yeates" /> The pre- and post-SET regions are adjacent to SET domain and are cysteine rich.<ref name="Schubert" /><ref name="Yeates" /> The pre-SET cysteine region is located near the N-terminal where the post-SET region is located near the C-terminal of the domain.<ref name="Schubert" /><ref name="Yeates" /> These regions are said to play an important role in substrate recognition and enzymatic activity.<ref name="Schubert" /><ref name="Yeates" /> The cysteine regions are not shown in the crystal structure as only residues 117-366 were crystalized.<ref name="Xiao" />		The ΔSET7/9 consists of the [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain] along with the pre- and post-SET regions.<ref name="Schubert" /><ref name="Yeates" /> The pre- and post-SET regions are adjacent to SET domain and are cysteine rich.<ref name="Schubert" /><ref name="Yeates" /> The pre-SET cysteine region is located near the N-terminal where the post-SET region is located near the C-terminal of the domain.<ref name="Schubert" /><ref name="Yeates" /> These regions are said to play an important role in substrate recognition and enzymatic activity.<ref name="Schubert" /><ref name="Yeates" /> The cysteine regions are not shown in the crystal structure as only residues 117-366 were crystalized.<ref name="Xiao" />

-	The SET domain is mostly defined by turns and loops, which connect secondary structures, with the few <scene name='81/811707/Beta_sheets/4'>antiparallel β-sheets</scene>.<ref name="Schubert" /> <scene name='81/811707/Beta-hairpin/3'>Residues 337-349</scene> form a β-hairpin that sticks out at a right angle to the surface of the enzyme.<ref name="Xiao" /> This hairpin stabilizes the conformation of tyrosine residues.<ref name="Xiao" /> The following three residues (<scene name='81/811707/Sharp_bend/3'>350-352</scene>) accommodate a unique sharp bend in the peptide chain and the end of the protein takes on an <scene name='81/811707/C-term_alpha_helix/2'>α-helical conformation</scene>.<ref name="Xiao" /> This alpha helix packs against a beta sheet and orients the cofactor towards the active site.<ref name="Xiao" /> The two most defining features of the SET domain are the C-terminal tyrosine and the <scene name='81/811707/Variable_knot/3'>knot-like fold</scene>. These two components have been recognized to be essential for S-adenosyl-L-methionine(SAM) binding and catalysis, which is shown as <scene name='81/811707/Sam_isolated/3'>S-adenosyl-L-homocysteine</scene>(SAH) in the structure after methylation of the histone.<ref name="Schubert" /> <ref name="Yeates" /> <ref name="Huang" /> The knot-like fold contains the binding sites for the cofactor SAM and the peptide substrate.<ref name="Licciardello" />	+	The SET domain is mostly defined by turns and loops, which connect secondary structures, with the few <scene name='81/811707/Beta_sheets/4'>antiparallel β-sheets</scene>.<ref name="Schubert" /> <scene name='81/811707/Beta-hairpin/3'>Residues 337-349</scene> form a β-hairpin that sticks out at a right angle to the surface of the enzyme.<ref name="Xiao" /> This hairpin stabilizes the conformation of tyrosine residues.<ref name="Xiao" /> The following three residues (<scene name='81/811707/Sharp_bend/4'>350-352</scene>) accommodate a unique sharp bend in the peptide chain and the end of the protein takes on an <scene name='81/811707/C-term_alpha_helix/2'>α-helical conformation</scene>.<ref name="Xiao" /> This alpha helix packs against a beta sheet and orients the cofactor towards the active site.<ref name="Xiao" /> The two most defining features of the SET domain are the C-terminal tyrosine and the <scene name='81/811707/Variable_knot/3'>knot-like fold</scene>. These two components have been recognized to be essential for S-adenosyl-L-methionine(SAM) binding and catalysis, which is shown as <scene name='81/811707/Sam_isolated/3'>S-adenosyl-L-homocysteine</scene>(SAH) in the structure after methylation of the histone.<ref name="Schubert" /> <ref name="Yeates" /> <ref name="Huang" /> The knot-like fold contains the binding sites for the cofactor SAM and the peptide substrate.<ref name="Licciardello" />

	[[Image:Methyl1.gif\|300 px\|right\|thumb\|Figure 2: Image of substrate bound on one side of SET7/9 (PDB 1o9s) with the lysine target in the active site channel (cyan) and S-adenosyl homocysteine (pink) bound on the opposite face of the enzyme]]		[[Image:Methyl1.gif\|300 px\|right\|thumb\|Figure 2: Image of substrate bound on one side of SET7/9 (PDB 1o9s) with the lysine target in the active site channel (cyan) and S-adenosyl homocysteine (pink) bound on the opposite face of the enzyme]]

Ashley Crotteau at 23:02, 25 April 2019

Ashley Crotteau — Thu, 25 Apr 2019 23:02:44 GMT

←Older revision		Revision as of 23:02, 25 April 2019
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	[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: Epigenetic overview. Showing the methylation of histones and how this affects DNA packing.<ref name="Epigenetics" />]]		[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: Epigenetic overview. Showing the methylation of histones and how this affects DNA packing.<ref name="Epigenetics" />]]

-	[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that have N- or C-terminal tails. These tails can be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin shown in Figure 1. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is ~~also~~ a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can ~~either~~ activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and ~~vise~~ versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.	+	[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that have N- or C-terminal tails. These tails can be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin shown in Figure 1. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vice versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in ''Homo sapiens''.<ref name="Biterge" /> The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.


	==Structure==		==Structure==

-	The human lysine methyltransferase(HKMT) SET7/9 is 366 amino acids long that comes from ''H. sapiens''. Structure has two proteins in the asymmetric unit, yet acts as a monomer. HKMT will crystalize as a dimer. The structure is composed of the ΔSET7/9 domain. There is a two-domain architecture containing a conserved anti-parallel 𝛃-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor, SAM, that plays a role in the active site. HKMT only monomethylates H3K4, because the tyrosine rich active site does not allow di- or tri- methylation.	+	The human lysine methyltransferase(HKMT) SET7/9 is 366 amino acids long that comes from ''H. sapiens''. Structure has two proteins in the asymmetric unit, yet acts as a monomer. HKMT will crystalize as a dimer. The structure is composed of the ΔSET7/9 domain. There is a two-domain architecture containing a conserved anti-parallel 𝛃-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor, SAM, that plays a role in the active site.<ref name="Biterge" /> HKMT only monomethylates H3K4, because the tyrosine rich active site does not allow for di- or tri- methylation.

	===SET Domain===		===SET Domain===

-	The ΔSET7/9 consists of the SET domain along with the pre- and post-SET regions.<ref name="Schubert" /><ref name="Yeates" /> The pre- and post-SET regions are adjacent to SET domain and are cysteine rich.<ref name="Schubert" /><ref name="Yeates" /> The pre-SET cysteine region is located near the N-terminal where the post-SET region is located near the C-terminal of the domain.<ref name="Schubert" /><ref name="Yeates" /> These regions are said to play an important role in substrate recognition and enzymatic activity.<ref name="Schubert" /><ref name="Yeates" /> The cysteine regions are not shown in the crystal structure as only residues 117-366 were crystalized.<ref name="Xiao" />	+	The ΔSET7/9 consists of the [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain] along with the pre- and post-SET regions.<ref name="Schubert" /><ref name="Yeates" /> The pre- and post-SET regions are adjacent to SET domain and are cysteine rich.<ref name="Schubert" /><ref name="Yeates" /> The pre-SET cysteine region is located near the N-terminal where the post-SET region is located near the C-terminal of the domain.<ref name="Schubert" /><ref name="Yeates" /> These regions are said to play an important role in substrate recognition and enzymatic activity.<ref name="Schubert" /><ref name="Yeates" /> The cysteine regions are not shown in the crystal structure as only residues 117-366 were crystalized.<ref name="Xiao" />

	The SET domain is mostly defined by turns and loops, which connect secondary structures, with the few <scene name='81/811707/Beta_sheets/4'>antiparallel β-sheets</scene>.<ref name="Schubert" /> <scene name='81/811707/Beta-hairpin/3'>Residues 337-349</scene> form a β-hairpin that sticks out at a right angle to the surface of the enzyme.<ref name="Xiao" /> This hairpin stabilizes the conformation of tyrosine residues.<ref name="Xiao" /> The following three residues (<scene name='81/811707/Sharp_bend/3'>350-352</scene>) accommodate a unique sharp bend in the peptide chain and the end of the protein takes on an <scene name='81/811707/C-term_alpha_helix/2'>α-helical conformation</scene>.<ref name="Xiao" /> This alpha helix packs against a beta sheet and orients the cofactor towards the active site.<ref name="Xiao" /> The two most defining features of the SET domain are the C-terminal tyrosine and the <scene name='81/811707/Variable_knot/3'>knot-like fold</scene>. These two components have been recognized to be essential for S-adenosyl-L-methionine(SAM) binding and catalysis, which is shown as <scene name='81/811707/Sam_isolated/3'>S-adenosyl-L-homocysteine</scene>(SAH) in the structure after methylation of the histone.<ref name="Schubert" /> <ref name="Yeates" /> <ref name="Huang" /> The knot-like fold contains the binding sites for the cofactor SAM and the peptide substrate.<ref name="Licciardello" />		The SET domain is mostly defined by turns and loops, which connect secondary structures, with the few <scene name='81/811707/Beta_sheets/4'>antiparallel β-sheets</scene>.<ref name="Schubert" /> <scene name='81/811707/Beta-hairpin/3'>Residues 337-349</scene> form a β-hairpin that sticks out at a right angle to the surface of the enzyme.<ref name="Xiao" /> This hairpin stabilizes the conformation of tyrosine residues.<ref name="Xiao" /> The following three residues (<scene name='81/811707/Sharp_bend/3'>350-352</scene>) accommodate a unique sharp bend in the peptide chain and the end of the protein takes on an <scene name='81/811707/C-term_alpha_helix/2'>α-helical conformation</scene>.<ref name="Xiao" /> This alpha helix packs against a beta sheet and orients the cofactor towards the active site.<ref name="Xiao" /> The two most defining features of the SET domain are the C-terminal tyrosine and the <scene name='81/811707/Variable_knot/3'>knot-like fold</scene>. These two components have been recognized to be essential for S-adenosyl-L-methionine(SAM) binding and catalysis, which is shown as <scene name='81/811707/Sam_isolated/3'>S-adenosyl-L-homocysteine</scene>(SAH) in the structure after methylation of the histone.<ref name="Schubert" /> <ref name="Yeates" /> <ref name="Huang" /> The knot-like fold contains the binding sites for the cofactor SAM and the peptide substrate.<ref name="Licciardello" />

Ashley Crotteau at 22:48, 25 April 2019

Ashley Crotteau — Thu, 25 Apr 2019 22:48:28 GMT

←Older revision		Revision as of 22:48, 25 April 2019
Line 7:		Line 7:
	[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: Epigenetic overview. Showing the methylation of histones and how this affects DNA packing.<ref name="Epigenetics" />]]		[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: Epigenetic overview. Showing the methylation of histones and how this affects DNA packing.<ref name="Epigenetics" />]]

-	[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that ~~often~~ have N- or C-terminal tails. These tails can ~~often~~ be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin shown in Figure 1. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.	+	[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that have N- or C-terminal tails. These tails can be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin shown in Figure 1. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.

Ashley Crotteau at 22:36, 25 April 2019

Ashley Crotteau — Thu, 25 Apr 2019 22:36:44 GMT

←Older revision		Revision as of 22:36, 25 April 2019
Line 61:		Line 61:
	<ref name="Marino">PMID: 16209651 </ref>		<ref name="Marino">PMID: 16209651 </ref>
	<ref name="Biterge" <ref> DOI: 10.15406/mojcsr.2016.03.00047</ref>		<ref name="Biterge" <ref> DOI: 10.15406/mojcsr.2016.03.00047</ref>
-	<ref name="Epigenetics <ref>https://www.whatisepigenetics.com/fundamentals/</ref>	+	<ref name="Epigenetics" <ref>https://www.whatisepigenetics.com/fundamentals/</ref>
	<references/>		<references/>

Ashley Crotteau at 22:34, 25 April 2019

Ashley Crotteau — Thu, 25 Apr 2019 22:34:57 GMT

←Older revision		Revision as of 22:34, 25 April 2019
Line 5:		Line 5:

	==Introduction==		==Introduction==
-	[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: Epigenetic overview. Showing the methylation of histones and how this affects DNA packing.]]	+	[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: Epigenetic overview. Showing the methylation of histones and how this affects DNA packing.<ref name="Epigenetics" />]]

	[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that often have N- or C-terminal tails. These tails can often be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin shown in Figure 1. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.		[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that often have N- or C-terminal tails. These tails can often be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin shown in Figure 1. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.
Line 61:		Line 61:
	<ref name="Marino">PMID: 16209651 </ref>		<ref name="Marino">PMID: 16209651 </ref>
	<ref name="Biterge" <ref> DOI: 10.15406/mojcsr.2016.03.00047</ref>		<ref name="Biterge" <ref> DOI: 10.15406/mojcsr.2016.03.00047</ref>
-	<ref name="Epigenetics <ref>https://www.whatisepigenetics.com/fundamentals/ ~~epigenetic marker~~</ref>	+	<ref name="Epigenetics <ref>https://www.whatisepigenetics.com/fundamentals/</ref>
	<references/>		<references/>

Ashley Crotteau at 22:33, 25 April 2019

Ashley Crotteau — Thu, 25 Apr 2019 22:33:27 GMT

←Older revision		Revision as of 22:33, 25 April 2019
Line 61:		Line 61:
	<ref name="Marino">PMID: 16209651 </ref>		<ref name="Marino">PMID: 16209651 </ref>
	<ref name="Biterge" <ref> DOI: 10.15406/mojcsr.2016.03.00047</ref>		<ref name="Biterge" <ref> DOI: 10.15406/mojcsr.2016.03.00047</ref>
		+	<ref name="Epigenetics <ref>https://www.whatisepigenetics.com/fundamentals/ epigenetic marker</ref>
	<references/>		<references/>

Ashley Crotteau at 21:15, 24 April 2019

Ashley Crotteau — Wed, 24 Apr 2019 21:15:53 GMT

←Older revision		Revision as of 21:15, 24 April 2019
Line 5:		Line 5:

	==Introduction==		==Introduction==
-	[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: ~~epigenetic~~ overview. Showing the methylation of histones and how this affects DNA packing.]]	+	[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: Epigenetic overview. Showing the methylation of histones and how this affects DNA packing.]]

	[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that often have N- or C-terminal tails. These tails can often be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin shown in Figure 1. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.		[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that often have N- or C-terminal tails. These tails can often be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin shown in Figure 1. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.

Ashley Crotteau at 21:15, 24 April 2019

Ashley Crotteau — Wed, 24 Apr 2019 21:15:21 GMT

←Older revision		Revision as of 21:15, 24 April 2019
Line 7:		Line 7:
	[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: epigenetic overview. Showing the methylation of histones and how this affects DNA packing.]]		[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: epigenetic overview. Showing the methylation of histones and how this affects DNA packing.]]

-	[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that often have N- or C-terminal tails. These tails can often be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.	+	[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that often have N- or C-terminal tails. These tails can often be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin shown in Figure 1. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.

Ashley Crotteau at 21:14, 24 April 2019

Ashley Crotteau — Wed, 24 Apr 2019 21:14:46 GMT

←Older revision		Revision as of 21:14, 24 April 2019
Line 3:		Line 3:
	<StructureSection load= '1o9s' size='350' frame='true' side='right' caption='H. sapiens KMT 1o9s' scene='81/811707/Overall_structure/1'>		<StructureSection load= '1o9s' size='350' frame='true' side='right' caption='H. sapiens KMT 1o9s' scene='81/811707/Overall_structure/1'>

-	~~[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: epigenetic overview. Showing the methylation of histones and how this affects DNA packing.]]~~	+
	==Introduction==		==Introduction==
		+	[[Image:Epigentics pic.png\|300 px\|right\|thumb\|Figure 1: epigenetic overview. Showing the methylation of histones and how this affects DNA packing.]]

	[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that often have N- or C-terminal tails. These tails can often be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.		[https://en.wikipedia.org/wiki/Histone Histones] are a family of proteins that condense DNA into chromatin, and is an octamer composed of two of each protein core; H2A, H2B, H3, and H4. Histones are a globular protein, that often have N- or C-terminal tails. These tails can often be subjected to modifications by enzymes. Methylation of histones is one of the four common histone modifications. Methylation is most common on long tails of H3 and H4 due to the tail being able to enter the active site.<ref name ="DesJarlais" /> A histone can be mono-, di-, or tri- methylated. Once the histone is methylated, the DNA goes from tightly bound heterochromatin to loosely packed euchromatin. The euchromatin allows RNA pol II to bind to the DNA and start transcription. <ref name="Marino" /> Histone methylation is also a major epigenetic marker, which can be passed down from generation to generation. An [https://www.whatisepigenetics.com/fundamentals/ epigenetic marker] affects the way that genes are expressed, and can either activate or repress DNA. Histone methylation is a major epigenetic marker because it has the ability to change heterochromatin to euchromatin, and vise versa. Alterations in markers have been associated with many diseases.<ref name="Xiao" /> Lysine Methyltrasferase SET7/9 (KMT) is an enzyme that methylates the histone 3 lysine 4 (H3K4) and plays a important role in the transcription of DNA in H. sapiens.<ref name="Biterge" /> It is composed of 259 residues and is a monomer containing a [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1273623/ SET domain]. There is a two-domain architecture containing a conserved anti-parallel β-barrel and an unusual knot-like structure that creates the active site. It also contains a cofactor that plays a role in the active site.The methylation of H3K4 results in transcriptional activation.<ref name="Biterge" /> The specific methylation of H3K4 does not result in a change in charge because it is a nonpolar group being added to the lysine. A change in charge could result in tighter bound heterochromatin.