Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA.

Mer G, Bochkarev A, Gupta R, Bochkareva E, Frappier L, Ingles CJ, Edwards AM, Chazin WJ
Cell. 2000 103 (3): 449-56

PMID: 11081631 · DOI:10.1016/s0092-8674(00)00136-7

Replication protein A (RPA), the nuclear ssDNA-binding protein in eukaryotes, is essential to DNA replication, recombination, and repair. We have shown that a globular domain at the C terminus of subunit RPA32 contains a specific surface that interacts in a similar manner with the DNA repair enzyme UNG2 and repair factors XPA and RAD52, each of which functions in a different repair pathway. NMR structures of the RPA32 domain, free and in complex with the minimal interaction domain of UNG2, were determined, defining a common structural basis for linking RPA to the nucleotide excision, base excision, and recombinational pathways of repairing damaged DNA. Our findings support a hand-off model for the assembly and coordination of different components of the DNA repair machinery.

MeSH Terms (23)

Amino Acid Sequence Binding Sites DNA DNA-Binding Proteins DNA Repair Helix-Loop-Helix Motifs Humans Macromolecular Substances Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Peptide Fragments Protein Binding Proteins Protein Structure, Secondary Protein Structure, Tertiary Recombinant Fusion Proteins Replication Protein A RNA-Binding Proteins RNA Polymerase I Saccharomyces cerevisiae Proteins Sequence Alignment Xeroderma Pigmentosum Group A Protein

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