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Publication : Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein.

First Author  Masuda Y Year  2002
Journal  J Biol Chem Volume  277
Issue  4 Pages  3040-6
PubMed ID  11711549 Mgi Jnum  J:73959
Mgi Id  MGI:2157239 Doi  10.1074/jbc.M110149200
Citation  Masuda Y, et al. (2002) Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein. J Biol Chem 277(4):3040-6
abstractText  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.
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