The human REV1 gene codes for a DNA template-dependent dCMP transferase
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چکیده
منابع مشابه
The human REV1 gene codes for a DNA template-dependent dCMP transferase.
DNA is frequently damaged by various physical and chemical agents. DNA damage can lead to mutations during replication. In the yeast Saccharomyces cerevisiae, the damage-induced mutagenesis pathway requires the Rev1 protein. We have isolated a human cDNA homologous to the yeast REV1 gene. The human REV1 cDNA consists of 4255 bp and codes for a protein of 1251 amino acid residues with a calculat...
متن کاملResponse of human REV1 to different DNA damage: preferential dCMP insertion opposite the lesion.
REV1 functions in the DNA polymerase zeta mutagenesis pathway. To help understand the role of REV1 in lesion bypass, we have examined activities of purified human REV1 opposite various template bases and several different DNA lesions. Lacking a 3'-->5' proofreading exonuclease activity, purified human REV1 exhibited a DNA polymerase activity on a repeating template G sequence, but catalyzed nuc...
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 کاملLesion bypass by human DNA polymerase mu reveals a template-dependent, sequence-independent nucleotidyl transferase activity.
DNA polymerase mu (pol mu), which is related to terminal deoxynucleotidyl transferase and DNA polymerase beta, is thought to be involved in non-homologous end joining and V(D)J recombination. Pol mu is induced by ionizing radiation and exhibits low fidelity. Analysis of translesion replication by purified human pol mu revealed that it bypasses a synthetic abasic site with high efficiency, using...
متن کاملDeoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain.
The REV1 protein is a member of the growing family of translesion DNA polymerases. A cDNA of the human REV1 gene that we had originally isolated encoded 1250 amino acids residues, which was one amino acid shorter than previously reported ones. The shorter form of REV1 was named REV1S. All individuals examined expressed equivalent amounts of REV1S and REV1 mRNA, suggesting that the REV1S mRNA is...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 1999
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/27.22.4468