JBC INTERFERin siRNA transfection reagent

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Volume 271, Number 51, Issue of December 20, 1996 pp. 32511-32514
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Cleavage Efficiency by Adenovirus Protease Is Site-dependent

(Received for publication, October 17, 1996)

Mounir Diouri , Hossein Keyvani-Amineh , Kieran F. Geoghegan Dagger and Joseph M. Weber

From the Department of Microbiology, Faculty of Medicine, University of Sherbrooke, Quebec, Canada J1H 5N4 and the Dagger  Department of Molecular Sciences, Central Research Division, Pfizer Inc., Groton, Connecticut 06340

The adenovirus protease cleaves consensus sequences (M/I/L)XGX-G and (M/I/L)XGG-X. Using purified recombinant protease, we showed that a peptide bearing the GX-G site was hydrolyzed more rapidly than a peptide bearing the GG-X site. The GX-G site was also preferentially cleaved on viral protein pVI which bears both sites of cleavage. Evidence is presented that suggests a biological role for this differential cleavage efficiency.


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