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PMID: 11205331 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

DNA polymerase iota and related rad30-like enzymes.

McDonald JP, Tissier A, Frank EG, Iwai S, Hanaoka F, Woodgate R

Abstract

Until recently, the molecular mechanisms of translesion DNA synthesis (TLS), a process whereby a damaged base is used as a template for continued replication, was poorly understood. This area of scientific research has, however, been revolutionized by the finding that proteins long implicated in TLS are, in fact, DNA polymerases. Members of this so-called UmuC/DinB/Rev1/Rad30 superfamily of polymerases have been identified in prokaryotes, eukaryotes and archaea. Biochemical studies with the highly purified polymerases reveal that some, but not all, can traverse blocking lesions in template DNA. All of them share a common feature, however, in that they exhibit low fidelity when replicating undamaged DNA. Of particular interest to us is the Rad30 subfamily of polymerases found exclusively in eukaryotes. Humans possess two Rad30 paralogs, Rad30A and Rad30B. The RAD30A gene encodes DNA polymerase eta and defects in the protein lead to the xeroderma pigmentosum variant (XP-V) phenotype in humans. Very recently RAD30B has also been shown to encode a novel DNA polymerase, designated as Pol iota. Based upon in vitro studies, it appears that Pol iota has the lowest fidelity of any eukaryotic polymerase studied to date and we speculate as to the possible cellular functions of such a remarkably error-prone DNA polymerase.

MeSH Terms
Bacterial Proteins/physiology DNA-Directed DNA Polymerase/physiology Escherichia coli Proteins Humans Proteins/physiology Saccharomyces cerevisiae/physiology
Chemicals
Bacterial Proteins DinB protein, E coli Escherichia coli Proteins Proteins UmuC protein, E coli DNA polymerase iota DNA-Directed DNA Polymerase POLK protein, human Rad30 protein
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
McDonald J P
Section on DNA Replication, Repair and Mutagenesis, National Institute of Child Health and Human Development, Bethesda, MD 20892-2725, USA.
Tissier A
Frank E G
Iwai S
Hanaoka F
Woodgate R
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Article Info
Journal
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
Abbr.
Philos Trans R Soc Lond B Biol Sci
ISSN
0962-8436
Published
2001-01-29
Pages
53-60
Language
English
Region
England
NLM ID
7503623
PMCID
PMC1087691
Subset
IM
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