4fjo - Revision history

OCA at 11:17, 1 March 2024

2024-03-01T11:17:13Z

←Older revision		Revision as of 11:17, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fjo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FJO FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fjo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FJO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.718Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjo OCA], [https://pdbe.org/4fjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fjo RCSB], [https://www.ebi.ac.uk/pdbsum/4fjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjo ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjo OCA], [https://pdbe.org/4fjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fjo RCSB], [https://www.ebi.ac.uk/pdbsum/4fjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref>		[https://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	DNA synthesis across lesions during genomic replication requires concerted actions of specialized DNA polymerases in a potentially mutagenic process known as translesion synthesis. Current models suggest that translesion synthesis in mammalian cells is achieved in two sequential steps, with a Y-family DNA polymerase (kappa, eta, iota, or Rev1) inserting a nucleotide opposite the lesion and with the heterodimeric B-family polymerase zeta, consisting of the catalytic Rev3 subunit and the accessory Rev7 subunit, replacing the insertion polymerase to carry out primer extension past the lesion. Effective translesion synthesis in vertebrates requires the scaffolding function of the C-terminal domain (CTD) of Rev1 that interacts with the Rev1-interacting region of polymerases kappa, eta, and iota and with the Rev7 subunit of polymerase zeta. We report the purification and structure determination of a quaternary translesion polymerase complex consisting of the Rev1 CTD, the heterodimeric Pol zeta complex, and the Pol kappa Rev1-interacting region. Yeast two-hybrid assays were employed to identify important interface residues of the translesion polymerase complex. The structural elucidation of such a quaternary translesion polymerase complex encompassing both insertion and extension polymerases bridged by the Rev1 CTD provides the first molecular explanation of the essential scaffolding function of Rev1 and highlights the Rev1 CTD as a promising target for developing novel cancer therapeutics to suppress translesion synthesis. Our studies support the notion that vertebrate insertion and extension polymerases could structurally cooperate within a megatranslesion polymerase complex (translesionsome) nucleated by Rev1 to achieve efficient lesion bypass without incurring an additional switching mechanism.

-	~~Structural basis of Rev1-mediated assembly of a quaternary vertebrate translesion~~ polymerase ~~complex consisting of Rev1, heterodimeric~~ polymerase (Pol) zeta, and Pol kappa.,Wojtaszek J, Lee CJ, D'Souza S, Minesinger B, Kim H, D'Andrea AD, Walker GC, Zhou P J Biol Chem. 2012 Sep 28;287(40):33836-46. Epub 2012 Aug 2. PMID:22859295<ref>PMID:22859295</ref>	+	==See Also==
-		+	*[[DNA polymerase 3D structures\|DNA polymerase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4fjo" style="background-color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:52, 19 October 2022

2022-10-19T19:52:41Z

←Older revision		Revision as of 19:52, 19 October 2022
Line 1:		Line 1:

	==Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex==		==Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex==
-	<StructureSection load='4fjo' size='340' side='right' caption='[[4fjo]], [[Resolution\|resolution]] 2.72Å' scene=''>	+	<StructureSection load='4fjo' size='340' side='right'caption='[[4fjo]], [[Resolution\|resolution]] 2.72Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fjo]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FJO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fjo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FJO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Rev1, Rev1l ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Polk, Dinb1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Mad2l2, Mad2b, Rev7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Rev3l, Polz, Sez4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjo OCA], [https://pdbe.org/4fjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fjo RCSB], [https://www.ebi.ac.uk/pdbsum/4fjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjo ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjo OCA], [~~http~~://pdbe.org/4fjo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fjo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fjo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjo ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http://www.uniprot.org/uniprot/DPOLZ_MOUSE DPOLZ_MOUSE]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis (By similarity). [[http~~://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref> [[http://www.uniprot.org/uniprot/MD2L2_MOUSE MD2L2_MOUSE]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation (By similarity). [[http://www.uniprot.org/uniprot/POLK_MOUSE POLK_MOUSE]] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).<ref>PMID:12432099</ref>	+	[https://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~DNA-directed DNA polymerase~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Lee, C J]]	+	[[Category: Lee C-J]]
-	[[Category: Wojtaszek, J]]	+	[[Category: Wojtaszek J]]
-	[[Category: Zhou, P]]	+	[[Category: Zhou P]]
-	~~[[Category: Transferase -dna binding protein complex]]~~	+
-	~~[[Category: Transferase-dna binding protein complex]]~~	+
-	~~[[Category: Translesion synthesis~~]]	+

OCA at 19:55, 24 January 2018

2018-01-24T19:55:31Z

←Older revision		Revision as of 19:55, 24 January 2018
Line 27:		Line 27:
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Lee, C J]]		[[Category: Lee, C J]]
-	[[Category: Wojtaszek, ~~Jessica~~]]	+	[[Category: Wojtaszek, J]]
	[[Category: Zhou, P]]		[[Category: Zhou, P]]
	[[Category: Transferase -dna binding protein complex]]		[[Category: Transferase -dna binding protein complex]]
	[[Category: Transferase-dna binding protein complex]]		[[Category: Transferase-dna binding protein complex]]
	[[Category: Translesion synthesis]]		[[Category: Translesion synthesis]]

OCA at 08:17, 15 November 2017

2017-11-15T08:17:41Z

←Older revision		Revision as of 08:17, 15 November 2017
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4fjo" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4fjo" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[DNA polymerase\|DNA polymerase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:52, 4 August 2016

2016-08-04T11:52:53Z

←Older revision		Revision as of 11:52, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex==		==Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex==
	<StructureSection load='4fjo' size='340' side='right' caption='[[4fjo]], [[Resolution\|resolution]] 2.72Å' scene=''>		<StructureSection load='4fjo' size='340' side='right' caption='[[4fjo]], [[Resolution\|resolution]] 2.72Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fjo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FJO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fjo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FJO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Rev1, Rev1l ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~]), Polk, Dinb1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~]), Mad2l2, Mad2b, Rev7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~]), Rev3l, Polz, Sez4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Rev1, Rev1l ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Polk, Dinb1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Mad2l2, Mad2b, Rev7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Rev3l, Polz, Sez4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fjo RCSB], [http://www.ebi.ac.uk/pdbsum/4fjo PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjo OCA], [http://pdbe.org/4fjo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fjo RCSB], [http://www.ebi.ac.uk/pdbsum/4fjo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4fjo" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Lee, C J]]		[[Category: Lee, C J]]
	[[Category: Wojtaszek, Jessica]]		[[Category: Wojtaszek, Jessica]]

OCA at 09:02, 25 December 2014

2014-12-25T09:02:15Z

←Older revision		Revision as of 09:02, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4fjo\| PDB=4fjo \| SCENE= }}~~	+	==Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex==
-	===Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex===	+	<StructureSection load='4fjo' size='340' side='right' caption='[[4fjo]], [[Resolution\|resolution]] 2.72Å' scene=''>
-	~~{{ABSTRACT_PUBMED_22859295}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4fjo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FJO FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Rev1, Rev1l ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), Polk, Dinb1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), Mad2l2, Mad2b, Rev7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), Rev3l, Polz, Sez4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fjo RCSB], [http://www.ebi.ac.uk/pdbsum/4fjo PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/DPOLZ_MOUSE DPOLZ_MOUSE]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis (By similarity). [[http://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref> [[http://www.uniprot.org/uniprot/MD2L2_MOUSE MD2L2_MOUSE]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation (By similarity). [[http://www.uniprot.org/uniprot/POLK_MOUSE POLK_MOUSE]] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).<ref>PMID:12432099</ref>		[[http://www.uniprot.org/uniprot/DPOLZ_MOUSE DPOLZ_MOUSE]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis (By similarity). [[http://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref> [[http://www.uniprot.org/uniprot/MD2L2_MOUSE MD2L2_MOUSE]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation (By similarity). [[http://www.uniprot.org/uniprot/POLK_MOUSE POLK_MOUSE]] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).<ref>PMID:12432099</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DNA synthesis across lesions during genomic replication requires concerted actions of specialized DNA polymerases in a potentially mutagenic process known as translesion synthesis. Current models suggest that translesion synthesis in mammalian cells is achieved in two sequential steps, with a Y-family DNA polymerase (kappa, eta, iota, or Rev1) inserting a nucleotide opposite the lesion and with the heterodimeric B-family polymerase zeta, consisting of the catalytic Rev3 subunit and the accessory Rev7 subunit, replacing the insertion polymerase to carry out primer extension past the lesion. Effective translesion synthesis in vertebrates requires the scaffolding function of the C-terminal domain (CTD) of Rev1 that interacts with the Rev1-interacting region of polymerases kappa, eta, and iota and with the Rev7 subunit of polymerase zeta. We report the purification and structure determination of a quaternary translesion polymerase complex consisting of the Rev1 CTD, the heterodimeric Pol zeta complex, and the Pol kappa Rev1-interacting region. Yeast two-hybrid assays were employed to identify important interface residues of the translesion polymerase complex. The structural elucidation of such a quaternary translesion polymerase complex encompassing both insertion and extension polymerases bridged by the Rev1 CTD provides the first molecular explanation of the essential scaffolding function of Rev1 and highlights the Rev1 CTD as a promising target for developing novel cancer therapeutics to suppress translesion synthesis. Our studies support the notion that vertebrate insertion and extension polymerases could structurally cooperate within a megatranslesion polymerase complex (translesionsome) nucleated by Rev1 to achieve efficient lesion bypass without incurring an additional switching mechanism.
		+
		+	Structural basis of Rev1-mediated assembly of a quaternary vertebrate translesion polymerase complex consisting of Rev1, heterodimeric polymerase (Pol) zeta, and Pol kappa.,Wojtaszek J, Lee CJ, D'Souza S, Minesinger B, Kim H, D'Andrea AD, Walker GC, Zhou P J Biol Chem. 2012 Sep 28;287(40):33836-46. Epub 2012 Aug 2. PMID:22859295<ref>PMID:22859295</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4fjo]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Mus_musculus Mus musculus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:022859295</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[DNA polymerase\|DNA polymerase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Lee, C J.]]	+	[[Category: Lee, C J]]
	[[Category: Wojtaszek, Jessica]]		[[Category: Wojtaszek, Jessica]]
-	[[Category: Zhou, P.]]	+	[[Category: Zhou, P]]
	[[Category: Transferase -dna binding protein complex]]		[[Category: Transferase -dna binding protein complex]]
	[[Category: Transferase-dna binding protein complex]]		[[Category: Transferase-dna binding protein complex]]
	[[Category: Translesion synthesis]]		[[Category: Translesion synthesis]]

OCA at 09:45, 19 June 2013

2013-06-19T09:45:51Z

←Older revision		Revision as of 09:45, 19 June 2013
Line 1:		Line 1:
-	[[Image:4fjo.jpg\|left\|200px]]
-
	{{STRUCTURE_4fjo\| PDB=4fjo \| SCENE= }}		{{STRUCTURE_4fjo\| PDB=4fjo \| SCENE= }}
-
	===Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex===		===Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex===
		+	{{ABSTRACT_PUBMED_22859295}}

		+	==Function==
		+	[[http://www.uniprot.org/uniprot/DPOLZ_MOUSE DPOLZ_MOUSE]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis (By similarity). [[http://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref> [[http://www.uniprot.org/uniprot/MD2L2_MOUSE MD2L2_MOUSE]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation (By similarity). [[http://www.uniprot.org/uniprot/POLK_MOUSE POLK_MOUSE]] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).<ref>PMID:12432099</ref>

	==About this Structure==		==About this Structure==
	[[4fjo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA].		[[4fjo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022859295</ref><references group="xtra"/><references/>
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]

OCA at 05:35, 8 August 2012

2012-08-08T05:35:51Z

←Older revision		Revision as of 05:35, 8 August 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4fjo.jpg\|left\|200px]]

-	~~The entry~~ 4fjo ~~is ON HOLD~~	+	{{STRUCTURE_4fjo\| PDB=4fjo \| SCENE= }}

-	~~Authors: Wojtaszek, Jessica, Lee, C.~~-~~J., Zhou, P.~~	+	===Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex===

-	~~Description:~~ Structure ~~of the Rev1 CTD~~-~~Rev3~~/7-~~Pol kappa RIR~~ complex	+
		+	==About this Structure==
		+	[[4fjo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA].
		+	[[Category: DNA-directed DNA polymerase]]
		+	[[Category: Mus musculus]]
		+	[[Category: Lee, C J.]]
		+	[[Category: Wojtaszek, Jessica]]
		+	[[Category: Zhou, P.]]
		+	[[Category: Transferase -dna binding protein complex]]
		+	[[Category: Transferase-dna binding protein complex]]
		+	[[Category: Translesion synthesis]]

OCA at 05:25, 27 June 2012

2012-06-27T05:25:06Z

←Older revision		Revision as of 05:25, 27 June 2012
Line 3:		Line 3:
	The entry 4fjo is ON HOLD		The entry 4fjo is ON HOLD

-	Authors: Wojtaszek, Jessica, Lee, ~~Chul~~-~~Jin~~, Zhou, ~~Pei~~	+	Authors: Wojtaszek, Jessica, Lee, C.-J., Zhou, P.

	Description: Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex		Description: Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex

OCA: Protected "4fjo" [edit=sysop:move=sysop]

2012-06-20T07:27:31Z

Protected "4fjo" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:27, 20 June 2012