Cleavage efficiency by adenovirus protease is site-dependent.
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.
Diouri
M
M
Department of Microbiology, Faculty of Medicine, University of Sherbrooke, Quebec, Canada J1H 5N4. j.weber@courrier.usherb.ca
Keyvani-Amineh
H
H
Geoghegan
K F
KF
Weber
J M
JM
D000260:Adenoviruses, Human / Q000201:enzymology*; D000595:Amino Acid Sequence; D002213:Capsid / Q000378:metabolism; D016384:Consensus Sequence; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism; D013379:Substrate Specificity
D011498:Protein Precursors; D010450:Endopeptidases; D003546:Cysteine Endopeptidases