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(Pol nu Fidelity)
 
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<Structure load='1bna' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_O'Brochta_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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<Structure load='4xvi' size='350' frame='true' align='right' caption='Pol nu' scene='' />
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==Your Heading Here (maybe something like 'Structure')==
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
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==DNA polymerase nu Function==
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== Disease ==
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<scene name='75/751199/Poln/1'>DNA polymerase nu</scene> is the most recently discovered DNA polymerase in the human genome. Pol nu is a family A polymerase meaning that it is either a replicative or repair polymerase. It is most closely related to Escherichia coli pol I, human POLQ, and Drosophila Mus308. Although the specific biological functions are unknown, it is known that Pol nu is related to DNA repair and homologous recombination. Additionally, Pol nu plays a role in DNA translesion synthesis. Pol nu can perform translesion synthesis past thymine glycol which is a product of reactive oxygen species damage to DNA. Pol nu is able to perform translesion synthesis past thymine glycol while thymine glycol blocks most DNA polymerases during synthesis.
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== Relevance ==
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==Pol nu Fidelity==
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== Structural highlights ==
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Pol nu is one of the types of polymerases that is conserved in vertebrates, but it is error-prone, meaning it has low base substitution fidelity. During the replication process in the nucleus, specifically as Pol nu interacts with the DNA molecule at the <scene name='75/751199/Helix/1'>O helix</scene> of the finger domain on the protein, it discriminates poorly against the misinsertion of dNTP, specifically for guanine against thymine on the <scene name='75/751199/Dna_attachment_to_protein/1'>DNA template molecule</scene>. Pol nu incorporates T opposite G on a template at a frequency of 0.45 which is a higher frequency than any other known DNA polymerase. This error is unusual for family A polymerases.
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
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== References ==
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<references/>
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Current revision

Pol nu

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DNA polymerase nu Function

is the most recently discovered DNA polymerase in the human genome. Pol nu is a family A polymerase meaning that it is either a replicative or repair polymerase. It is most closely related to Escherichia coli pol I, human POLQ, and Drosophila Mus308. Although the specific biological functions are unknown, it is known that Pol nu is related to DNA repair and homologous recombination. Additionally, Pol nu plays a role in DNA translesion synthesis. Pol nu can perform translesion synthesis past thymine glycol which is a product of reactive oxygen species damage to DNA. Pol nu is able to perform translesion synthesis past thymine glycol while thymine glycol blocks most DNA polymerases during synthesis.

Pol nu Fidelity

Pol nu is one of the types of polymerases that is conserved in vertebrates, but it is error-prone, meaning it has low base substitution fidelity. During the replication process in the nucleus, specifically as Pol nu interacts with the DNA molecule at the of the finger domain on the protein, it discriminates poorly against the misinsertion of dNTP, specifically for guanine against thymine on the . Pol nu incorporates T opposite G on a template at a frequency of 0.45 which is a higher frequency than any other known DNA polymerase. This error is unusual for family A polymerases.

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