Leucine repeats in the large subunit of herpes simplex virus type 2 ribonucleotide reductase (RR; ICP10) are involved in RR activity and subunit complex formation.
Computer-assisted comparison of the herpes simplex virus type 2 (HSV-2) ribonucleotide reductase large subunit (RR1) sequence with the known primary structures of other RR1 proteins revealed a motif consisting of five leucines occurring at every seventh residue between positions 409 to 437. This motif is specific to HSV RR1 proteins. A synthetic oligopeptide (LA-4) corresponding to 15 residues in the internal portion of the motif inhibited HSV-2 RR activity. In immunoprecipitation experiments, LA-4 disrupted a complex consisting of RR1, the small RR subunit and a previously uncharacterized 180K protein, apparently of cellular origin. We deduce that the LA-4 sequence represents a critical RR1 site involved in RR complex formation and enzymic activity.
Chung
T D
TD
Department of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, Baltimore 21201.
Luo
J H
JH
Wymer
J P
JP
Smith
C C
CC
Aurelian
L
L
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D005814:Genes, Viral; D007930:Leucine / Q000235:genetics*; D008969:Molecular Sequence Data; D011233:Precipitin Tests; D012091:Repetitive Sequences, Nucleic Acid; D012264:Ribonucleotide Reductases / Q000037:antagonists & inhibitors / Q000235:genetics* / Q000378:metabolism; D018139:Simplexvirus / Q000201:enzymology / Q000235:genetics*
D000911:Antibodies, Monoclonal; D012264:Ribonucleotide Reductases; D007930:Leucine