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The mutation frequency in AtPolzeta-, AtRev1- or AtPoleta-knockout plants rev3-1, rev1-1 and polh (show POLH Proteins)-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.
Rev1 could serve as a backup polymerase in base excision repair and could potentially contribute to activation-induced cytidine deaminase (show AICDA Proteins)-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 (show PCNA Proteins)oubiquitylation after UV radiation through interacting with ubiquitylated RAD18.
Rev1 is essential for the Msh2 (show MSH2 Proteins)-independent generation of these transversions downstream of Ung2 (show UNG Proteins)-induced apyrimidinic sites.
Rev1 operates in the same pathway as Ung (show UNG Proteins), as emphasized by further decreased CSR (show SCARA3 Proteins) in Rev1(-/-)Msh2 (show MSH2 Proteins)(-/-) 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 (show POLL Proteins)
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 (show POLH Proteins) 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 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 (show PCNA Proteins) monoubiquitylation after UV radiation through interacting with ubiquitylated RAD18 (show RAD18 Proteins).
Data suggest that relatively high affinity binding of PolD3 (show POLD3 Proteins)-RIR (show APBB1 Proteins) motif to Rev1-C-terminal domain displaces subunits from PolN, Pol-iota (show POLM Proteins), or PolK (show PAPD7 Proteins) from Rev1 complex and promotes formation of Rev1/PolZ4 assembly with PCNA (show PCNA Proteins) for translesion DNA replication.
Rev1 is indispensable for Translesion synthesis mediated by Poleta, Poliota, and Polkappa (show POLL Proteins) but is not required for TLS (show FUS Proteins) 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 (show TP53 Proteins) 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.
The results show that human Rev1 disrupts G4 DNA structures and prevents refolding in vitro.
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