Structure of a mutant form of proliferating cell nuclear antigen that blocks translesion DNA synthesis.

ABSTRACT: Proliferating cell nuclear antigen (PCNA) is a homotrimeric protein that functions as a sliding clamp during DNA replication. Several mutant forms of PCNA that block translesion DNA synthesis have been identified in genetic studies in yeast. One such mutant protein (encoded by the rev6-1 allele) is a glycine to serine substitution at residue 178, located at the subunit interface of PCNA. To improve our understanding of how this substitution interferes with translesion synthesis, we have determined the X-ray crystal structure of the PCNA G178S mutant protein. This substitution has little effect on the structure of the domain in which the substitution occurs. Instead, significant, local structural changes are observed in the adjacent subunit. The most notable difference between mutant and wi

SUBMITTER: Freudenthal BD 

PROVIDER: S-EPMC2703463 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature