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J Gen Virol 72 (1991), 1139-1144; DOI 10.1099/0022-1317-72-5-1139
© 1991 Society for General Microbiology
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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

Theodore D. Chung1, JianHua Luo1, James P. Wymer1, Cynthia C. Smith1,2 and Laure Aurelian1,2

1 Virology/Immunology Laboratories, Department of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, Baltimore, Maryland 21201
and2 Departments of Biochemistry and Comparative Medicine, The Johns Hopkins Medical Institutions, Baltimore, Maryland 21205, U.S.A.

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.

Received 16 October 1990; accepted 27 January 1991.


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Copyright © 1991 by the Society for General Microbiology.