Identification of a novel REV1-interacting motif necessary for DNA polymerase κ function
نویسندگان
چکیده
منابع مشابه
Human Rev1 polymerase disrupts G-quadruplex DNA
The Y-family DNA polymerase Rev1 is required for successful replication of G-quadruplex DNA (G4 DNA) in higher eukaryotes. Here we show that human Rev1 (hRev1) disrupts G4 DNA structures and prevents refolding in vitro. Nucleotidyl transfer by hRev1 is not necessary for mechanical unfolding to occur. hRev1 binds G4 DNA substrates with Kd,DNA values that are 4-15-fold lower than those of non-G4 ...
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seen in this study for verbs, in the processing of time and temporal structure [10]. While Shapiro et al. [3] are admirably restrained in their interpretations, they outline how their results suggest there is some relationship between grammatical class and semantic representations. This is a far from trivial issue: from a classic psycho-linguistic perspective, semantic and syntactic representat...
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DNA interstrand crosslinks (ICLs) are covalent linkages between two strands of DNA, and their presence interferes with essential metabolic processes such as transcription and replication. These lesions are extremely toxic, and their repair is essential for genome stability and cell survival. In this review, we will discuss how the removal of ICLs requires interplay between multiple genome maint...
متن کاملYeast Rev1 protein is a G template-specific DNA polymerase.
Rev1 protein of Saccharomyces cerevisiae functions with DNA polymerase zeta in mutagenic trans-lesion synthesis. Because of the reported preferential incorporation of a C residue opposite an abasic site, Rev1 has been referred to as a deoxycytidyltransferase. Here, we use steady-state kinetics to examine nucleotide incorporation by Rev1 opposite undamaged and damaged template residues. We show ...
متن کاملNMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase η.
Rev1 is a translesion synthesis (TLS) DNA polymerase essential for DNA damage tolerance in eukaryotes. In the process of TLS stalled high-fidelity replicative DNA polymerases are temporarily replaced by specialized TLS enzymes that can bypass sites of DNA damage (lesions), thus allowing replication to continue or postreplicational gaps to be filled. Despite its limited catalytic activity, human...
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ژورنال
عنوان ژورنال: Genes to Cells
سال: 2009
ISSN: 1356-9597,1365-2443
DOI: 10.1111/j.1365-2443.2008.01255.x