Structure of PolC reveals unique DNA binding and fidelity determinants (Q27653260)

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Douglas R Davies

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James M Bullard

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Jeffrey Christensen

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Louis S Green

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Joseph W Guiles

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Wendy K Ribble

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Nebojsa Janjic

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Thale C Jarvis

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

30 December 2008

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published in

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volume

105

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issue

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page(s)

20695-700

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cites work

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An error-prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses a 'steric gate' residue for discrimination against ribonucleotides

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Active site directed inhibitors of replication-specific bacterial DNA polymerases

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Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity

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Genetic identification of two distinct DNA polymerases, DnaE and PolC, that are essential for chromosomal DNA replication in Staphylococcus aureus.

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Evolution of dnaQ, the gene encoding the editing 3' to 5' exonuclease subunit of DNA polymerase III holoenzyme in Gram-negative bacteria

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A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously.

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Conserved interactions in the Staphylococcus aureus DNA PolC chromosome replication machine

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DNA polymerase III of Gram-positive eubacteria is a zinc metalloprotein conserving an essential finger-like domain

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PubMed

https://pubmed.ncbi.nlm.nih.gov/19106298

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19106298

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.0809989106

1 reference

ADS bibcode

2008PNAS..10520695E

0 references

1 reference

1 reference

PubMed publication ID

19106298

1 reference