Open AccessDominant negative rat DNA polymerase beta mutants interfere with base excision repair in Saccharomyces cerevisiae
Author(s) -
Caroline Clairmont,
Joann B. Sweasy
Publication year - 1996
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.178.3.656-661.1996
Subject(s) - biology , dna polymerase , nucleotide excision repair , base excision repair , polymerase , microbiology and biotechnology , dna polymerase i , saccharomyces cerevisiae , dna repair , dna polymerase ii , dna polymerase beta , mutant , dna clamp , dna , biochemistry , gene , polymerase chain reaction , reverse transcriptase
DNA polymerase beta is one of the smallest known eukaryotic DNA polymerases. This polymerase has been very well characterized in vitro, but its functional role in vivo has yet to be determined. Using a novel competition assay in Escherichia coli, we isolated two DNA polymerase beta dominant negative mutants. When we overexpressed the dominant negative mutant proteins in Saccharomyces cerevisiae, the cells became sensitive to methyl methanesulfonate. Interestingly, overexpression of the same polymerase beta mutant proteins did not confer sensitivity to UV damage, strongly suggesting that the mutant proteins interfere with the process of base excision repair but not nucleotide excision repair in S. cerevisiae. Our data implicate a role for polymerase IV, the S. cerevisiae polymerase beta homolog, in base excision repair in S. cerevisiae.