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