Cloned mouse ribonucleotide reductase subunit M1 cDNA reveals amino acid sequence homology with Escherichia coli and herpesvirus ribonucleotide reductases.
We have isolated and sequenced overlapping cDNA clones containing the entire coding region of mouse ribonucleotide reductase subunit M1. The coding region comprises 2.4 kilobases and predicts a polypeptide of 792 amino acids (Mr 90,234) which shows striking homology with ribonucleotide reductases from Escherichia coli and the herpesviruses, Epstein-Barr virus and herpes simplex virus. The homologies reveal three domains: an N-terminal domain common to the mammalian and bacterial enzymes, a C-terminal domain common to the mammalian and viral ribonucleotide reductases, and a central domain common to all three. We speculate on the functional basis of this conservation.
Caras
I W
IW
Levinson
B B
BB
Fabry
M
M
Williams
S R
SR
Martin
D W
DW
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis*; D004926:Escherichia coli / Q000201:enzymology*; D004854:Herpesvirus 4, Human / Q000201:enzymology; D046911:Macromolecular Substances; D051379:Mice; D011061:Poly A / Q000378:metabolism; D012313:RNA / Q000378:metabolism; D012333:RNA, Messenger; D012264:Ribonucleotide Reductases / Q000235:genetics*; D018139:Simplexvirus / Q000201:enzymology*
D046911:Macromolecular Substances; D012333:RNA, Messenger; D011061:Poly A; D012313:RNA; D004247:DNA; D012264:Ribonucleotide Reductases