ArticleBiochemistry2008
Structure of a mutant form of proliferating cell nuclear antigen that blocks translesion DNA synthesis.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 31 citations in OpenAlex.
- Structural Basis for the Interaction Between Yeast Chromatin Assembly Factor 1 and Proliferating Cell Nuclear Antigen.Journal of molecular biology · 2024Article
- Photo-activatable Ub-PCNA probes reveal new structural features of the Saccharomyces cerevisiae Polη/PCNA complex.Nucleic acids research · 2021Article
- Interdomain connecting loop and J loop structures determine cross-species compatibility of PCNA.The Journal of biological chemistry · 2021Article
- Article
- PCNA tool belts and polymerase bridges form during translesion synthesis.Nucleic acids research · 2016Article
- The Proliferating Cell Nuclear Antigen (PCNA)-interacting Protein (PIP) Motif of DNA Polymerase η Mediates Its Interaction with the C-terminal Domain of Rev1.The Journal of biological chemistry · 2016Article
- Identification of New Mutations at the PCNA Subunit Interface that Block Translesion Synthesis.PloS one · 2016Article
- Dead-End Elimination with a Polarizable Force Field Repacks PCNA Structures.Biophysical journal · 2015Article
- Effects of polymorphisms in translesion DNA synthesis genes on lung cancer risk and prognosis in Chinese men.Cancer epidemiology · 2013Article
- Distinct structural alterations in proliferating cell nuclear antigen block DNA mismatch repair.Biochemistry · 2013Article
- PCNA trimer instability inhibits translesion synthesis by DNA polymerase η and by DNA polymerase δ.DNA repair · 2013Article
- Unligated Okazaki Fragments Induce PCNA Ubiquitination and a Requirement for Rad59-Dependent Replication Fork Progression.PloS one · 2013Article
- PCNA structure and function: insights from structures of PCNA complexes and post-translationally modified PCNA.Sub-cellular biochemistry · 2012Review
- Solution X-ray scattering combined with computational modeling reveals multiple conformations of covalently bound ubiquitin on PCNA.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The non-canonical protein binding site at the monomer-monomer interface of yeast proliferating cell nuclear antigen (PCNA) regulates the Rev1-PCNA interaction and Polζ/Rev1-dependent translesion DNA synthesis.The Journal of biological chemistry · 2011Article
- Crystal structure of SUMO-modified proliferating cell nuclear antigen.Journal of molecular biology · 2011Article
- Processivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesis.Biochimica et biophysica acta · 2010Review
- Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange.Nature structural & molecular biology · 2010Article
- Chemically ubiquitylated PCNA as a probe for eukaryotic translesion DNA synthesis.Nature chemical biology · 2010Article
- A charged residue at the subunit interface of PCNA promotes trimer formation by destabilizing alternate subunit interactions.Acta crystallographica. Section D, Biological crystallography · 2009Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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 wild-type structures is in a single, extended loop (comprising amino acid residues 105-110), which we call loop J. In the mutant protein structure, loop J adopts a very different conformation in which the atoms of the protein backbone have moved by as much as 6.5 A from their positions in the wild-type structure. To improve our understanding of the functional consequences of this structural change, we have examined the ability of this mutant protein to stimulate nucleotide incorporation by DNA polymerase eta (pol eta). Steady state kinetic studies show that while wild-type PCNA stimulates incorporation by pol eta opposite an abasic site, the mutant PCNA protein actually inhibits incorporation opposite this DNA lesion. These results show that the position of loop J in PCNA plays an essential role in facilitating translesion synthesis.
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