Reference - Detail
|Author||Masuda Y, Takahashi M, Fukuda S, Sumii M, Kamiya K.|
|Title||Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein.|
|Journal||J Biol Chem|
The Rev1 protein, a member of a large family of translesion DNA polymerases, catalyzes a dCMP transfer reaction. Recombinant mouse Rev1 protein was found to insert a dCMP residue opposite guanine, adenine, thymine, cytosine, uracil, and an apurinic/apyrimidinic site and to have weak ability for transfer to a mismatched terminus. The mismatch-extension ability was strongly enhanced by a guanine residue on the template near the mismatched terminus; this was not the case with an apurinic/apyrimidinic site and the other template nucleotides. Kinetic analysis of the dCMP transferase reaction provided evidence for high affinity for dCTP with template G but not the other templates, whereas the template nucleotide did not much affect the V(max) value. Furthermore, it could be established that the mouse Rev1 protein inserts dGMP and dTMP residues opposite template guanine at a V(max) similar to that for dCMP.
|MeSH||Amino Acid Sequence Animals Base Pair Mismatch Binding Sites Blotting, Northern Centrifugation, Density Gradient DNA Repair DNA, Complementary / metabolism Deoxycytidine Monophosphate / metabolism* Deoxyguanine Nucleotides / metabolism Electrophoresis, Polyacrylamide Gel Fungal Proteins / metabolism* Guanine / chemistry Humans Kinetics Mice Mice, Inbred C57BL Molecular Sequence Data Mutation Nucleotidyltransferases* Protein Binding Protein Structure, Tertiary Recombinant Proteins / metabolism Saccharomyces cerevisiae Proteins* Sequence Homology, Amino Acid Tissue Distribution|
|WOS Category||BIOCHEMISTRY & MOLECULAR BIOLOGY|
|Prokaryotes E. coli||?ME9042(BL21(DE3))|