نتایج جستجو برای: بروسلاملیتنسیس rev1

تعداد نتایج: 346  

Journal: :Nucleic acids research 2002
Yanbin Zhang Xiaohua Wu Olga Rechkoblit Nicholas E Geacintov John-Stephen Taylor Zhigang Wang

REV1 functions in the DNA polymerase zeta mutagenesis pathway. To help understand the role of REV1 in lesion bypass, we have examined activities of purified human REV1 opposite various template bases and several different DNA lesions. Lacking a 3'-->5' proofreading exonuclease activity, purified human REV1 exhibited a DNA polymerase activity on a repeating template G sequence, but catalyzed nuc...

Journal: :Biochemistry 2012
Alexandra Pozhidaeva Yulia Pustovalova Sanjay D'Souza Irina Bezsonova Graham C Walker Dmitry M Korzhnev

Rev1 is a translesion synthesis (TLS) DNA polymerase essential for DNA damage tolerance in eukaryotes. In the process of TLS stalled high-fidelity replicative DNA polymerases are temporarily replaced by specialized TLS enzymes that can bypass sites of DNA damage (lesions), thus allowing replication to continue or postreplicational gaps to be filled. Despite its limited catalytic activity, human...

Journal: :Nucleic acids research 1999
W Lin H Xin Y Zhang X Wu F Yuan Z Wang

DNA is frequently damaged by various physical and chemical agents. DNA damage can lead to mutations during replication. In the yeast Saccharomyces cerevisiae, the damage-induced mutagenesis pathway requires the Rev1 protein. We have isolated a human cDNA homologous to the yeast REV1 gene. The human REV1 cDNA consists of 4255 bp and codes for a protein of 1251 amino acid residues with a calculat...

Journal: :Nucleic Acids Research 2005
Anna-Laura Ross Laura J. Simpson Julian E. Sale

REV1 is central to the DNA damage response of eukaryotes through an as yet poorly understood role in translesion synthesis. REV1 is a member of the Y-type DNA polymerase family and is capable of in vitro deoxycytidyl transferase activity opposite a range of damaged bases. However, non-catalytic roles for REV1 have been suggested by the Saccharomyces cerevisiae rev1-1 mutant, which carries a poi...

2015
Masashi Uchiyama Junko Terunuma Fumio Hanaoka Giovanni Maga

Translesion DNA synthesis provides an alternative DNA replication mechanism when template DNA is damaged. In fission yeast, Eso1 (polη), Kpa1/DinB (polκ), Rev1, and Polζ (a complex of Rev3 and Rev7) have been identified as translesion synthesis polymerases. The enzymatic characteristics and protein-protein interactions of these polymerases have been intensively characterized; however, how these...

2016
Rajendra Prasad Vladimir Poltoratsky Esther W. Hou Samuel H. Wilson

Rev1 is a member of the Y-family of DNA polymerases and is known for its deoxycytidyl transferase activity that incorporates dCMP into DNA and its ability to function as a scaffold factor for other Y-family polymerases in translesion bypass events. Rev1 also is involved in mutagenic processes during somatic hypermutation of immunoglobulin genes. In light of the mutation pattern consistent with ...

2015
Simon M. Langer Kristina Hopfensperger Shilpa S. Iyer Edward F. Kreider Gerald H. Learn Lan-Hui Lee Beatrice H. Hahn Daniel Sauter Massimo Caputi

BACKGROUND Pandemic strains of HIV-1 (group M) encode a total of nine structural (gag, pol, env), regulatory (rev, tat) and accessory (vif, vpr, vpu, nef) genes. However, some subtype A and C viruses exhibit an unusual gene arrangement in which the first exon of rev (rev1) and the vpu gene are placed in the same open reading frame. Although this rev1-vpu gene fusion is present in a considerable...

Journal: :The Journal of biological chemistry 2006
Yuji Masuda Kenji Kamiya

Cellular functions of the REV1 gene have been conserved in evolution and appear important for maintaining genetic integrity through translesion DNA synthesis. This study documents a novel biochemical activity of human REV1 protein, due to higher affinity for single-stranded DNA (ssDNA) than the primer terminus. Preferential binding to long ssDNA regions of the template strand means that REV1 is...

Journal: :The Journal of biological chemistry 2002
Lajos Haracska Satya Prakash Louise Prakash

Rev1 protein of Saccharomyces cerevisiae functions with DNA polymerase zeta in mutagenic trans-lesion synthesis. Because of the reported preferential incorporation of a C residue opposite an abasic site, Rev1 has been referred to as a deoxycytidyltransferase. Here, we use steady-state kinetics to examine nucleotide incorporation by Rev1 opposite undamaged and damaged template residues. We show ...

Journal: :Nucleic Acids Research 2005
Jacob G. Jansen Anastasia Tsaalbi-Shtylik Petra Langerak Fabienne Calléja Caro M. Meijers Heinz Jacobs Niels de Wind

Rev1 is a deoxycytidyl transferase associated with DNA translesion synthesis (TLS). In addition to its catalytic domain, Rev1 possesses a so-called BRCA1 C-terminal (BRCT) domain. Here, we describe cells and mice containing a targeted deletion of this domain. Rev1(B/B) mice are healthy, fertile and display normal somatic hypermutation. Rev1(B/B) cells display an elevated spontaneous frequency o...

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