1 Structural basis of Rev 1 - mediated assembly of a quaternary vertebrate translesion polymerase complex consisting of Rev 1 , heterodimeric Pol and
نویسندگان
چکیده
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA Dana-Farber Cancer Institute, 450 Brookline Avenue, Boston, MA 02215, USA These authors contributed equally to this work. Running title: Structure of the Rev1 CTD-Rev3/7-Pol RIR complex To whom correspondence should be addressed: Pei Zhou, Dept. of Biochemistry, Duke University Medical Center, Durham, NC, 27710, USA. Tel.: (919) 668-6409; Fax: (919) 684-8885; E-mail: [email protected]
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Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase ζ and REV1
DNA polymerase ζ (Polζ) is an error-prone DNA polymerase involved in translesion DNA synthesis (TLS). Polζ consists of two subunits: the catalytic REV3, which belongs to B-family DNA polymerase, and the non-catalytic REV7. REV7 also interacts with REV1 polymerase, which is an error-prone Y-family DNA polymerase and also involved in TLS. Cells deficient in one of the three REV proteins and those...
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