Journal
MOLECULAR CELL
Volume 28, Issue 6, Pages 1058-1070Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2007.10.025
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Funding
- NCI NIH HHS [R01 CA021615-30, R01 CA021615, CA021615] Funding Source: Medline
- NIEHS NIH HHS [P30 ES002109] Funding Source: Medline
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DinB is the only translesion Y family DNA polymerase conserved among bacteria, archaea, and eukaryotes. DinB and its orthologs possess a specialized lesion bypass function but also display potentially deleterious -1 frameshift mutagenic phenotypes when overproduced. We show that the DNA damage-inducible proteins UmuD(2) and RecA act in concert to modulate this mutagenic activity. Structural modeling suggests that the relatively open active site of DinB is enclosed by interaction with these proteins, thereby preventing the template bulging responsible for -1 frameshift mutagenesis. Intriguingly, residues that define the UmuD(2)- interacting surface on Dinl3 statistically covary throughout evolution, suggesting a driving force for the maintenance of a regulatory protein-protein interaction at this site. Together, these observations indicate that proteins like RecA and UmuD(2) may be responsible for managing the mutagenic potential of DinB orthologs throughout evolution.
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