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| - | {{Sandbox_Reserved_O'Brochta_HLSC322}}<!-- | + | {{Sandbox_Reserved_O'Brochta_HLSC322}}<!-- DNA Polymerase I --> |
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==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' /> | ||
| - | The discovery of DNA Polymerase I is credited to Arthur Kornberg in 1955. Kornberg and his colleagues isolated RNA pol I from ''E. coli'' extracts through a DNA assay. '''SOURCE''' This enzyme was the first DNA polymerase discovered, and was therefore given the name DNA Polymerase I. | + | The discovery of DNA Polymerase I is credited to Arthur Kornberg in 1955. Kornberg and his colleagues isolated RNA pol I from ''E. coli'' extracts through a DNA assay. '''SOURCE''' This enzyme was the first DNA polymerase discovered, and was therefore given the name DNA Polymerase I. It plays a key role in prokaryotic DNA replication. |
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| + | ==Function== | ||
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| + | 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. The active site in this function is found in the Klenow Fragment which contains both the polymerase and exonuclease active sites. '''SOURCE Proteopedia''' | ||
| - | 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. | ||
Revision as of 20:55, 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
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The discovery of DNA Polymerase I is credited to Arthur Kornberg in 1955. Kornberg and his colleagues isolated RNA pol I from E. coli extracts through a DNA assay. SOURCE This enzyme was the first DNA polymerase discovered, and was therefore given the name DNA Polymerase I. It plays a key role in prokaryotic DNA replication.
Function
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. The active site in this function is found in the Klenow Fragment which contains both the polymerase and exonuclease active sites. SOURCE Proteopedia
Its function is parallel to the eukaryotic DNA polymerase BLANK.
Sources
Lehman, I. R. (2003). Discovery of DNA polymerase. Journal of Biological Chemistry, 278(37), 34733-34738.
