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PMID: 11861920 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

UV-induced T-->C transition at a TT photoproduct site is dependent on Saccharomyces cerevisiae polymerase eta in vivo.

Nucleic acids research ·Vol. 30 ·No. 5 ·2002-03-01 ·Pages 1262-7

Zhang H, Siede W

Abstract

UV-induced reversion of the arg4-17 ochre allele in Saccharomyces cerevisiae is largely dependent on translesion polymerase eta (Rad30p), known to bypass cyclobutane-type TT dimers in an error-free fashion. arg4-17 locus reversion was predominantly due to T-->C transition of T127, the 3' T of a TT photoproduct site. This event was at least 20-fold reduced in a rad30 deletion mutant, irrespective of the status of nucleotide excision repair. These data correlate with known properties of 6-4 TT photoproducts and in vitro characteristics of polymerase eta and suggest that polymerase eta plays an important in vivo role in inserting G opposite the 3' T of 6-4 TT photoproducts at this site. Alternatively, an unprecedented error-prone processing of cyclobutane-type photoproducts at this site by polymerase eta must be assumed as the critical mechanism. Whereas photoreactivation results indeed hint at the latter possibility, a possible regulatory influence of reducing the overall UV damage load on the bypass probability of non-cyclobutane-type pyrimidine dimer photoproducts should not be dismissed.

MeSH Terms
Argininosuccinate Lyase Base Sequence Cell Division/radiation effects DNA Damage DNA Repair DNA, Fungal/chemistry DNA-Directed DNA Polymerase/genetics,physiology Deoxycytosine Nucleotides/metabolism Dose-Response Relationship, Radiation Fungal Proteins/genetics Mutation Nucleic Acid Conformation Pyrimidine Dimers/metabolism Saccharomyces cerevisiae/enzymology,genetics,radiation effects Saccharomyces cerevisiae Proteins Thymine Nucleotides/metabolism Ultraviolet Rays
Chemicals
DNA, Fungal Deoxycytosine Nucleotides Fungal Proteins Pyrimidine Dimers Saccharomyces cerevisiae Proteins Thymine Nucleotides DNA-Directed DNA Polymerase Rad30 protein Arg4 protein, S cerevisiae Argininosuccinate Lyase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Zhang Hong
Department of Radiation Oncology and Winship Cancer Institute, B5111, Emory University School of Medicine, 1365 B Clifton Road NE, Atlanta, GA 30322, USA.
Siede Wolfram
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
1362-4962
DOI
10.1093/nar/30.5.1262
Published
2002-03-01
Pages
1262-7
Language
English
Region
England
NLM ID
0411011
PMCID
PMC101249
Subset
IM
Grants
NCI NIH HHS · R01 CA087381 · United States
NCI NIH HHS · CA87381 · United States
External Links
PubMed source DOI: 10.1093/nar/30.5.1262 PMC Full Text View journal details
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