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Medientyp:
E-Artikel
Titel:
Determination of the substrate specificity of turnip mosaic virus NIa protease using a genetic method
Beteiligte:
Kang, Hara;
Lee, Yong Jae;
Goo, Jae Hwan;
Park, Woo Jin
Erschienen:
Microbiology Society, 2001
Erschienen in:
Journal of General Virology, 82 (2001) 12, Seite 3115-3117
Sprache:
Englisch
DOI:
10.1099/0022-1317-82-12-3115
ISSN:
0022-1317;
1465-2099
Entstehung:
Anmerkungen:
Beschreibung:
The RNA genome of turnip mosaic potyvirus (TuMV) encodes a large polyprotein that is processed to mature proteins by virus-encoded proteases. The TuMV NIa protease is responsible for the cleavage of the polyprotein at seven different locations. These cleavage sites are defined by a conserved sequence motif Val-Xaa-His-Gln↓, with the scissile bond located after Gln. To determine the substrate specificity of the NIa protease, amino acid sequences cleaved by the NIa protease were obtained from randomized sequence libraries using a screening method referred to as GASP (geneticassay forsite-specificproteolysis). Based on statistical analysis of the obtained sequences, a consensus substrate sequence was deduced: Yaa-Val-Arg-His-Gln↓Ser, with Yaa being an aliphatic amino acid and the scissile bond being located between Gln and Ser. This result is consistent with the conserved cleavage sequence motif, and should provide insight into the molecular activity of the NIa protease.