Abstract
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.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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DNA Damage
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DNA Replication
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism
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DNA-Directed DNA Polymerase / chemistry*
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DNA-Directed DNA Polymerase / genetics
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DNA-Directed DNA Polymerase / metabolism*
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Humans
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In Vitro Techniques
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Mad2 Proteins
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Models, Molecular
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Nuclear Magnetic Resonance, Biomolecular
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Nuclear Proteins / chemistry*
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Nucleotidyltransferases / chemistry*
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Nucleotidyltransferases / genetics
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Nucleotidyltransferases / metabolism*
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Protein Interaction Domains and Motifs
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Protein Subunits
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Proteins / chemistry*
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Proteins / genetics
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Proteins / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Thermodynamics
Substances
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DNA-Binding Proteins
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MAD2L2 protein, human
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Mad2 Proteins
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Nuclear Proteins
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Protein Subunits
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Proteins
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Recombinant Proteins
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DNA polymerase zeta
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Nucleotidyltransferases
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REV1 protein, human
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DNA-Directed DNA Polymerase
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REV3L protein, human
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Rad30 protein