The C-terminal domain of human Rev1 contains independent binding sites for DNA polymerase η and Rev7 subunit of polymerase ζ.
Human Rev1 is a translesion synthesis (TLS) DNA polymerase involved in bypass replication across sites of DNA damage and postreplicational gap-filling. Rev1 plays an essential structural role in TLS by providing a binding platform for other TLS polymerases that insert nucleotides across DNA lesions (polη, polι, polκ) and extend the ... distorted primer-terminus (polς). We use NMR spectroscopy to demonstrate that the Rev1 C-terminal domain utilizes independent interaction interfaces to simultaneously bind a fragment of the 'inserter' polη and Rev7 subunit of the 'extender' polς, thereby serving as a cassette that may accommodate several polymerases making them instantaneously available for TLS.
Mesh Terms:
Binding Sites, DNA Damage, DNA Replication, DNA-Binding Proteins, DNA-Directed DNA Polymerase, Humans, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Nuclear Proteins, Nucleotidyltransferases, Protein Interaction Domains and Motifs, Protein Subunits, Proteins, Recombinant Proteins, Thermodynamics
Binding Sites, DNA Damage, DNA Replication, DNA-Binding Proteins, DNA-Directed DNA Polymerase, Humans, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Nuclear Proteins, Nucleotidyltransferases, Protein Interaction Domains and Motifs, Protein Subunits, Proteins, Recombinant Proteins, Thermodynamics
FEBS Lett.
Date: Sep. 21, 2012
PubMed ID: 22828282
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