The C-Terminal Domain of Yeast PCNA Is Required for Physical And Functional Interactions With Cdc9 DNA Ligase
作者： Sangeetha Vijayakumar , Brian R. Chapados , Kristina H. Schmidt , Richard D. Kolodner , John A. Tainer
DOI: 10.1093/NAR/GKM006
关键词: dnaN 、 DNA ligase 、 Replication factor C 、 DNA mismatch repair 、 RFC2 、 DNA clamp 、 Okazaki fragments 、 Biology 、 DNA replication 、 Biochemistry
摘要: There is compelling evidence that proliferating cell nuclear antigen (PCNA), a DNA sliding clamp, co-ordinates the processing and joining of Okazaki fragments during eukaryotic replication. However, detailed mechanistic understanding functional PCNA:ligase I interactions has been incomplete. Here we present co-crystal structure yeast PCNA with peptide encompassing conserved interaction motif Cdc9, ligase I. The Cdc9 contacts both inter-domain connector loop (IDCL) residues near C-terminus PCNA. Complementary mutational biochemical results demonstrate these two interfaces are required for complex formation in absence when topologically linked to DNA. Similar functionally homologous human proteins, RFC interacts inhibits whereas addition alleviates inhibition by RFC. show ability overcome RFC-mediated dependent upon IDCL C-terminal Together significance β-zipper formed between domain reveal differences FEN-1 may contribute co-ordinated, sequential action enzymes.
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