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| + | {{Sandbox_Reserved_O'Brochta_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==DNA Polymerase I== | ==DNA Polymerase I== | ||
<Structure load='3ez5' size='350' frame='true' align='right' caption='DNA Polymerase I' scene='Insert optional scene name here' /> | <Structure load='3ez5' size='350' frame='true' align='right' caption='DNA Polymerase I' scene='Insert optional scene name here' /> | ||
| - | + | DNA Polymerase I is a key enzyme in prokaryotic DNA replication. Its primary role is removing the RNA primers initially laid down by DNA primase and replacing those nucleotides with dNTPs. The initial step of excising RNA nucleotides on the replicated strand is made possible due to its 3' to 5' exonuclease activity. | |
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| + | ==Structure== | ||
| + | DNA Polymerase I is a hetero trimer comprised of six chains with three distinct sequences. Each of the sequences is repeated twice within the molecule. Two of the six chains are polypeptide chains, each comprised of 580 amino acids. They have identical secondary structures with 31 alpha helices and 20 beta pleated sheets. Another distinct sequence found in DNA Polymerase is a short polypeptide chain that is 9 amino acids in length. The final distinct sequence is a DNA sequence that is 12 nucleotides in length. Each lengthy DNA chain has a condensed tertiary structure. A short | ||
==Function== | ==Function== | ||
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| - | Its primary role is removing the RNA primers initially laid down by the RNA polymerase primase and replacing those nucleotides with dNTPs. The initial step of excising RNA nucleotides on the replicated strand is made possible due to its 5' to 3' exonuclease activity. | ||
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| - | DNA polymerase I also has polymerase activity and 3' to 5' exonuclease activity. Both of the active sites for these functions are found in the Klenow Fragment. '''Clip thing''' | ||
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| - | The active site in this function is found in the Klenow Fragment which contains both the polymerase and 3' to 5' exonuclease active sites. '''SOURCE Proteopedia''' | ||
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Its function is parallel to the eukaryotic DNA polymerase '''BLANK'''. | Its function is parallel to the eukaryotic DNA polymerase '''BLANK'''. | ||
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| - | <scene name='75/751160/Dna/1'>DNA</scene> | ||
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| - | ==Sources== | ||
| - | Lehman, I. R. (2003). Discovery of DNA polymerase. Journal of Biological Chemistry, 278(37), 34733-34738. | ||
Revision as of 21:21, 8 February 2017
Contents |
genetics is ok
'Molecules it Interacts With and where '
The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.
PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
PHENYLALANINE
MAGNESIUM ION
'Origin'
It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.
'Structure'
It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.
Specific are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.
which play a crucial role in binding to the ribosome during translation. They form positive pockets with which negative amino acids can bind to.
'Molecules it Interacts With and where '
The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.
PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
PHENYLALANINE
MAGNESIUM ION
'Origin'
It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.
'Structure'
It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.
Specific are highlighted here.
which play a crucial role in binding to the ribosome during translation.
'Function"
The protein complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome by promoting GTP-dependent binding of tRNA to the A site of the ribosome. In other words, it is involved with elongation during polypeptide synthesis.
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DNA Polymerase I
|
DNA Polymerase I is a key enzyme in prokaryotic DNA replication. Its primary role is removing the RNA primers initially laid down by DNA primase and replacing those nucleotides with dNTPs. The initial step of excising RNA nucleotides on the replicated strand is made possible due to its 3' to 5' exonuclease activity.
Structure
DNA Polymerase I is a hetero trimer comprised of six chains with three distinct sequences. Each of the sequences is repeated twice within the molecule. Two of the six chains are polypeptide chains, each comprised of 580 amino acids. They have identical secondary structures with 31 alpha helices and 20 beta pleated sheets. Another distinct sequence found in DNA Polymerase is a short polypeptide chain that is 9 amino acids in length. The final distinct sequence is a DNA sequence that is 12 nucleotides in length. Each lengthy DNA chain has a condensed tertiary structure. A short
Function
Its function is parallel to the eukaryotic DNA polymerase BLANK.
