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The mutation frequency in AtPolzeta-, AtRev1- or AtPoleta-knockout plants rev3 (显示 REV3L 抗体)-1, rev1-1 and polh (显示 POLH 抗体)-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 (显示 AICDA 抗体)-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 mon (显示 PCNA 抗体)oubiquitylation after UV radiation through interacting with ubiquitylated RAD18.
Rev1 is essential for the Msh2 (显示 MSH2 抗体)-independent generation of these transversions downstream of Ung2 (显示 UNG 抗体)-induced apyrimidinic sites.
Rev1 operates in the same pathway as Ung (显示 UNG 抗体), as emphasized by further decreased CSR (显示 SCARA3 抗体) in Rev1(-/-)Msh2 (显示 MSH2 抗体)(-/-) 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 (显示 POLL 抗体)
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 (显示 POLH 抗体) and identify an alternative pathway in the generation of C to G and G to C transversions.
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 (显示 PCNA 抗体) monoubiquitylation after UV radiation through interacting with ubiquitylated RAD18 (显示 RAD18 抗体).
Data suggest that relatively high affinity binding of PolD3 (显示 POLD3 抗体)-RIR (显示 APBB1 抗体) motif to Rev1-C-terminal domain displaces subunits from PolN, Pol-iota (显示 POLM 抗体), or PolK (显示 PAPD7 抗体) from Rev1 complex and promotes formation of Rev1/PolZ4 assembly with PCNA (显示 PCNA 抗体) for translesion DNA replication.
Rev1 is indispensable for Translesion synthesis mediated by Poleta, Poliota, and Polkappa (显示 POLL 抗体) but is not required for TLS (显示 FUS 抗体) 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 (显示 TP53 抗体) 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
Structural studies suggest the possible involvement of XRCC1 and its associated repair factors, REV1 in post replication repair.
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