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REV1 homolog

Rev1, Rev1p
This gene encodes a protein with similarity to the S. cerevisiae mutagenesis protein Rev1. The Rev1 proteins contain a BRCT domain, which is important in protein-protein interactions. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: POLYMERASE, REV3, FUS, CAN, REV7
Papers on Rev1
Mutagenic Bypass of an Oxidized Abasic Lesion-Induced DNA Interstrand Cross-Link Analogue by Human Translesion Synthesis DNA Polymerases.
Zhao et al., Baltimore, United States. In Biochemistry, Jan 2016
Herein, we examined the capabilities of several highly relevant eukaryotic TLS DNA polymerases (pols), including human pol η, pol κ, pol ι, pol ν, REV1, and yeast pol ζ, to bypass this DOB-ICL analogue.
Requirement for Host RNA-Silencing Components and the Virus-Silencing Suppressor when Second-Site Mutations Compensate for Structural Defects in the 3' Untranslated Region.
Simon et al., College Park, United States. In J Virol, Dec 2015
All tested second-site mutations improved accumulation of TCV in conjunction with a partial reversion of the primary mutation (TCV-rev1) but had neutral or a negative effect on wild-type (wt) TCV or TCV with the primary mutation.
Contiguous 2,2,4-triamino-5(2H)-oxazolone obstructs DNA synthesis by DNA polymerases α, β, η, ι, κ, REV1 and Klenow Fragment exo-, but not by DNA polymerase ζ.
Miyazawa et al., Shizuoka, Japan. In J Biochem, Nov 2015
In this study, we analysed translesion synthesis (TLS) across two contiguous Oz molecules (OzOz) using Klenow Fragment exo(-) (KF exo(-)) and DNA polymerases (Pols) α, β, ζ, η, ι, κ and REV1.
FANCD2 and REV1 cooperate in the protection of nascent DNA strands in response to replication stress.
Guo et al., Beijing, China. In Nucleic Acids Res, Oct 2015
REV1 is a eukaryotic member of the Y-family of DNA polymerases involved in translesion DNA synthesis and genome mutagenesis.
MAD2L2 controls DNA repair at telomeres and DNA breaks by inhibiting 5' end resection.
Jacobs et al., Amsterdam, Netherlands. In Nature, Jun 2015
These activities of MAD2L2 depend on ATM kinase activity, RNF8, RNF168, 53BP1 and RIF1, but not on PTIP, REV1 and REV3, the latter two acting with MAD2L2 in translesion synthesis.
Transcriptome Analysis of Thermal Parthenogenesis of the Domesticated Silkworm.
Meng et al., Hangzhou, China. In Plos One, 2014
Some DEGs related to reactive oxygen species removal, DNA repair and heat shock response were differentially expressed between the two lines, such as MPV-17, REV1 and HSP68.
A Naturally Occurring rev1-vpu Fusion Gene Does Not Confer a Fitness Advantage to HIV-1.
Sauter et al., Ulm, Germany. In Plos One, 2014
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.
Error-free versus mutagenic processing of genomic uracil--relevance to cancer.
Slupphaug et al., Trondheim, Norway. In Dna Repair (amst), 2014
In addition, kataegis, localized hypermutations in one strand in the vicinity of genomic rearrangements, requires APOBEC protein, UNG2 and translesion polymerase REV1.
REV1 and DNA polymerase zeta in DNA interstrand crosslink repair.
Canman et al., Ann Arbor, United States. In Environ Mol Mutagen, 2012
It is now well recognized that translesion DNA synthesis (TLS), especially through the activities of REV1 and DNA polymerase zeta (Polζ), is necessary for both ICL repair pathways operating throughout the cell cycle.
Crystallization and X-ray diffraction analysis of the ternary complex of the C-terminal domain of human REV1 in complex with REV7 bound to a REV3 fragment involved in translesion DNA synthesis.
Hashimoto et al., Yokohama, Japan. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
ternary complex of the C-terminal domain of human REV1 in complex with REV7 bound to a REV3 fragment has been crystallized. The crystals belonged to space group P3(1)21, with unit-cell parameters a = b = 74.7, c = 124.5 A
Multifaceted recognition of vertebrate Rev1 by translesion polymerases ζ and κ.
Zhou et al., Durham, United States. In J Biol Chem, 2012
two distinct surfaces of the Rev1 C-terminal domain that separately mediate the assembly of extension and insertion translesion polymerase complexes
The vital role of polymerase ζ and REV1 in mutagenic, but not correct, DNA synthesis across benzo[a]pyrene-dG and recruitment of polymerase ζ by REV1 to replication-stalled site.
Moriya et al., Stony Brook, United States. In J Biol Chem, 2012
REV7 subunit of pol zeta mediated the interaction between REV3 and the REV1 C terminus.
Analysis of mice deficient in both REV1 catalytic activity and POLH reveals an unexpected role for POLH in the generation of C to G and G to C transversions during Ig gene hypermutation.
Wang et al., Yokohama, Japan. In Int Immunol, 2012
These results reveal genetic interactions between REV1 catalytic activity and POLH and identify an alternative pathway in the generation of C to G and G to C transversions.
Regulation of Rev1 by the Fanconi anemia core complex.
D'Andrea et al., Boston, United States. In Nat Struct Mol Biol, 2012
FAAP20 binding stabilizes Rev1 nuclear foci and promotes interaction of the Fanconi anemia core with PCNA-Rev1 DNA damage bypass complexes.
Ubiquitin-dependent regulation of translesion polymerases.
Jin et al., Hong Kong, Hong Kong. In Biochem Soc Trans, 2010
REV1 plays a central role in TLS because it interacts with all other Y-family members and Pol zeta.
DNA polymerase zeta: new insight into eukaryotic mutagenesis and mammalian embryonic development.
Zhang et al., Hangzhou, China. In World J Gastroenterol, 2003
Human REV3 amino acid residues 1 776-2 195 provide a REV7 binding domain, and REV7 amino acid residues 1-211 provide a bind domain for REV1, REV3 and REV7 itself.
Induction of somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase iota.
Weill et al., Paris, France. In Nature, 2002
The Y family of DNA polymerases--pol eta, pol iota, pol kappa and rev1--are specialized for copying DNA lesions and have high rates of error when copying a normal DNA template.
Cellular roles of DNA polymerase zeta and Rev1 protein.
Lawrence, Rochester, United States. In Dna Repair (amst), 2002
The majority of both spontaneous and DNA damage-induced mutations in eukaryotes result from replication processes in which DNA polymerase zeta (Polzeta) and Rev1 protein (Rev1p) play major roles.
Deoxycytidyl transferase activity of yeast REV1 protein.
Hinkle et al., Rochester, United States. In Nature, 1996
Mutagenesis induced by DNA damage in Saccharomyces cerevisiae requires the products of the REV1, REV3 and REV7 genes.
The Drosophila roughened mutation: activation of a rap homolog disrupts eye development and interferes with cell determination.
Rubin et al., Berkeley, United States. In Cell, 1991
Drosophila Rap1 protein is 88% identical to human rap1A/K-rev1 protein, a putative antagonist of ras action.
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