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抗Mouse (Murine) REV1 抗体:
抗Human REV1 抗体:
抗Rat (Rattus) REV1 抗体:
Human Polyclonal REV1 Primary Antibody for ELISA - ABIN547091
Masuda, Takahashi, Tsunekuni, Minami, Sumii, Miyagawa, Kamiya: Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain. in The Journal of biological chemistry 2001
The mutation frequency in AtPolzeta-, AtRev1- or AtPoleta-knockout plants rev3-1, rev1-1 and polh-1, respectively, were analyzed.
Arabidopsis thaliana disruptants of AtREV3, AtREV1, and/or AtPOLH genes that encode Translesion synthesis-type polymerases.
A translesion synthesis mechanism exists in higher plants and AtREV1 and AtREV7 have important roles in tolerating exposure to DNA-damaging agents. [AtREV1]
A study was conducted to clarify the function of REV1 by in vitro analysis using a primer extension assay.
Transgenic plants that over-expressed or disrupted REV1 showed reduced germination percentage, but the former exhibited a higher stem growth rate than the wild type during development.
These data indicate that dysregulation of cellular Rev1 levels leads to the accumulation of mutations and suppression of cell death, which accelerates the tumorigenic activities of DNA-damaging agents.
Rev1 could serve as a backup polymerase in base excision repair and could potentially contribute to activation-induced cytidine deaminase-initiated antibody diversification through this activity.
The results support the idea that Rev1 is not essential for the cellular translesion DNA synthesis functions of DNA polymerase zeta in mammalian cells.
REV1 promote PCNA monoubiquitylation after UV radiation through interacting with ubiquitylated RAD18.
Rev1 is essential for the Msh2-independent generation of these transversions downstream of Ung2-induced apyrimidinic sites.
Rev1 operates in the same pathway as Ung, as emphasized by further decreased CSR in Rev1(-/-)Msh2(-/-) B cells.
Structural basis of Rev1-mediated assembly of a quaternary vertebrate translesion polymerase complex consisting of Rev1, heterodimeric polymerase (Pol) zeta, and Pol kappa
REV1 and Polkappa are involved in DNA damage tolerance via Poleta-REV1 interaction when Poleta fails to bypass its cognate substrates.
two distinct surfaces of the Rev1 C-terminal domain that separately mediate the assembly of extension and insertion translesion polymerase complexes
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.
REV7 subunit of pol zeta mediated the interaction between REV3 and the REV1 C terminus.
The BRCT domain of Rev1 is involved in regulating DNA replication during the mutagenic bypass of spontaneous and induced DNA lesions.
REV1 expression is required for the methyl methanesulfonate induced mutagenesis phenotype of Pol beta null mouse embryonic fibroblast cells.
Results indicate a catalytic role of Rev1 in incorporating deoxycytidine residues, most likely opposite abasic nucleotides, during somatic hypermutation.
REV3 and REV1 play major roles in recombination-independent repair of DNA interstrand cross-links mediated by monoubiquitinated PCNA
Here, we report that mouse REV1 can bind directly to PCNA and that monoubiquitylation of PCNA enhances this interaction.
The REV1-interaction is essential for Polkappa function in vivo.
REV1 is implicated in the development of carcinogen-induced lung cancer.
Rev1-mediated DNA damage bypass at postreplicative gaps quenches irreversible DNA damage responses.
role for REV1 in the generation of C:G transitions and A:T mutations suggests that REV1 is involved in multiple mutagenic pathways through functional interaction with other polymerases during the hypermutation pro
results provide insights into the structure of the Rev1/Polzeta TLS assembly and highlight the function of Rev7 homo- and heterodimerization.
The data directly show that, in the human genome, DNA Pol-eta and Rev1 bypass cyclobutane pyrimidine dimers and 6-4PP at replication forks, while only 6-4PP are also tolerated by a Rev3L-dependent gap-filling mechanism, independent of S phase.
the catalytic function of REV1 is moderately or slightly altered by at least nine genetic variations, and the G4 DNA processing function of REV1 is slightly enhanced by the N373S variation, which might provide the possibility that certain germline missense REV1 variations affect the individual susceptibility to carcinogenesis by modifying the capability of REV1 for replicative bypass past DNA lesions and G4 motifs derived
REV1 can promote PCNA monoubiquitylation after UV radiation through interacting with ubiquitylated RAD18.
Data suggest that relatively high affinity binding of PolD3-RIR motif to Rev1-C-terminal domain displaces subunits from PolN, Pol-iota, or PolK from Rev1 complex and promotes formation of Rev1/PolZ4 assembly with PCNA for translesion DNA replication.
Rev1 is indispensable for Translesion synthesis mediated by Poleta, Poliota, and Polkappa but is not required for TLS by Polzeta.
Data suggest Rev1 protein recognition mechanism by Fanconi anemia-associated protein 20 (FAAP20).
show that REV1 is a novel binding partner of the tumor suppressor p53 and regulates its activity
Our results suggest for the first time that REV1 and REV3L SNPs might serve as potential predictive markers of outcome of cisplatin-based chemotherapy
The molecular mechanism of 3-nitrobenzanthrone genotoxicity in HEK293 cells is reported.
Structural studies suggest the possible involvement of XRCC1 and its associated repair factors, REV1 in post replication repair.
The results show that human Rev1 disrupts G4 DNA structures and prevents refolding in vitro.
the first structural insights into the regulation of human Rev1 for TLS polymerases.
Rev1 but not Poleta depletion is epistatic to the lack of PCNA ubiquitination.
analysis of the crystal structure of the ternary complex composed of the C-terminal domain of human REV1, REV7, and a REV3 fragment
a structural basis for understanding the recognition of the Rev1-CT by Y-family DNA polymerases
the Rev1 C-terminal domain utilizes independent interaction interfaces to simultaneously bind a fragment of the 'inserter' poleta and Rev7 subunit of the 'extender' polvarsigma, thereby serving as a cassette that may accommodate several polymerases
Findings indicate that miR-96 regulates DNA repair and chemosensitivity by repressing RAD51 and REV1.
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.
DNA repair protein REV1
, rev1-like terminal deoxycytidyl transferase
, REV1 homolog
, REV1- like
, alpha integrin-binding protein 80