title: The unique N-terminal domain of the large subunit of herpes simplex virus ribonucleotide reductase is preferentially sensitive to proteolysis.
abstract: 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.
authors.affiliation: MRC Virology Unit, University of Glasgow, U.K.
authors.forename: H
authors.initials: H
authors.lastname: Lankinen
authors.forename: E
authors.initials: E
authors.lastname: Telford
authors.forename: D
authors.initials: D
authors.lastname: MacDonald
authors.forename: H
authors.initials: H
authors.lastname: Marsden
mesh_terms: 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
chemical_list: D010446:Peptide Fragments; D012264:Ribonucleotide Reductases