The unique N-terminal domain of the large subunit of herpes simplex virus ribonucleotide reductase is preferentially sensitive to proteolysis.
Using antisera made against peptides corresponding to different regions of the large subunit of herpes simplex virus type 1 ribonucleotide reductase we have probed proteolytic fragments of this protein and found that at least a part of its unique N-terminal domain is not necessary for enzyme activity. This non-essential region encompasses the domain previously predicted to be composed of beta sheets with a well buried core of hydrophobic residues. Truncated forms of the large subunit are generated in vivo and are located almost exclusively in the nucleus.
Lankinen
H
H
MRC Virology Unit, University of Glasgow, U.K.
Telford
E
E
MacDonald
D
D
Marsden
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001345:Autoradiography; D015153:Blotting, Western; D002467:Cell Nucleus / Q000201:enzymology; D002999:Clone Cells; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism*; D012264:Ribonucleotide Reductases / Q000235:genetics / Q000378:metabolism*; D018139:Simplexvirus / Q000201:enzymology* / Q000235:genetics / Q000648:ultrastructure; D014709:Vero Cells
D010446:Peptide Fragments; D012264:Ribonucleotide Reductases