Premium
Y‐family DNA polymerases respond to DNA damage‐independent inhibition of replication fork progression
Author(s) -
Godoy Veronica G,
Jarosz Daniel F,
Walker Fabianne L,
Simmons Lyle A,
Walker Graham C
Publication year - 2006
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600986
Subject(s) - biology , dna replication , genetics , dna polymerase , replication (statistics) , fork (system call) , dna , replisome , eukaryotic dna replication , dna polymerase ii , control of chromosome duplication , microbiology and biotechnology , gene , virology , polymerase chain reaction , reverse transcriptase , computer science , operating system
In Escherichia coli , the Y‐family DNA polymerases Pol IV (DinB) and Pol V (UmuD 2 ′C) enhance cell survival upon DNA damage by bypassing replication‐blocking DNA lesions. We report a unique function for these polymerases when DNA replication fork progression is arrested not by exogenous DNA damage, but with hydroxyurea (HU), thereby inhibiting ribonucleotide reductase, and bringing about damage‐independent DNA replication stalling. Remarkably, the umuC122 ∷Tn 5 allele of umuC , dinB , and certain forms of umuD gene products endow E. coli with the ability to withstand HU treatment (HU R ). The catalytic activities of the UmuC122 and DinB proteins are both required for HU R . Moreover, the lethality brought about by such stalled replication forks in the wild‐type derivatives appears to proceed through the toxin/antitoxin pairs mazEF and relBE . This novel function reveals a role for Y‐family polymerases in enhancing cell survival under conditions of nucleotide starvation, in addition to their established functions in response to DNA damage.