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• W2029422499 endingPage "3105" @default.
• W2029422499 startingPage "3091" @default.
• W2029422499 abstract "Rev1 is a Y-family translesion synthesis (TLS) DNA polymerase involved in bypass replication across sites of DNA damage and postreplicational gap filling. In the process of TLS, high-fidelity replicative DNA polymerases stalled by DNA damage are replaced by error-prone TLS enzymes responsible for the majority of mutagenesis in eukaryotic cells. The polymerase exchange that gains low-fidelity TLS polymerases access to DNA is mediated by their interactions with proliferating cell nuclear antigen (PCNA). Rev1 stands alone from other Y-family TLS enzymes since it lacks the consensus PCNA-interacting protein box (PIP-box) motif, instead utilizing other modular domains for PCNA binding. Here we report solution NMR structure of an 11-kDa BRCA1 C-terminus (BRCT) domain from Saccharomyces cerevisiae Rev1 and demonstrate with the use of transverse relaxation optimized spectroscopy (TROSY) NMR methods that Rev1-BRCT domain directly interacts with an 87-kDa PCNA in solution. The domain adopts α/β fold (β1-α1-β2-β3-α2-β4-α3-α4) typical for BRCT domain superfamily. PCNA-binding interface of the Rev1-BRCT domain comprises conserved residues of the outer surface of the α1-helix and the α1-β1, β2-β3 and β3-α2 loops. On the other hand, Rev1-BRCT binds to the inter-domain region of PCNA that overlaps with the binding site for the PIP-box motif. Furthermore, Rev1-BRCT domain bound to PCNA can be displaced by increasing amounts of the PIP-box peptide from TLS DNA polymerase polη, suggesting that Rev1-BRCT and polη PIP-box interactions with the same PCNA monomer are mutually exclusive. These results provide structural insights into PCNA recognition by TLS DNA polymerases that help better understand TLS regulation in eukaryotes." @default.
• W2029422499 created "2016-06-24" @default.
• W2029422499 creator A5008065534 @default.
• W2029422499 creator A5075089490 @default.
• W2029422499 creator A5083844605 @default.
• W2029422499 date "2013-09-01" @default.
• W2029422499 modified "2023-09-27" @default.
• W2029422499 title "NMR Mapping of PCNA Interaction with Translesion Synthesis DNA Polymerase Rev1 Mediated by Rev1-BRCT Domain" @default.
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• W2029422499 doi "https://doi.org/10.1016/j.jmb.2013.05.029" @default.
• W2029422499 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23747975" @default.
• W2029422499 hasPublicationYear "2013" @default.
• W2029422499 type Work @default.
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• W2029422499 citedByCount "42" @default.

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