1887

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Volume 83, Issue 12

Characterization of a protein from with serine proteinase-like activity Free

Abstract

The RNA genome of (RTSV) is predicted to be expressed as a large polyprotein precursor (Shen ., 193, 621–630, 1993 ). The polyprotein is processed by at least one virus-encoded protease located adjacent to the C-terminal putative RNA polymerase which shows sequence similarity to viral serine-like proteases. The catalytic activity of this protease was explored using transcription/translation systems. Besides acting , the protease had activity on precursors containing regions of the 3’ half of the polyprotein but did not process a substrate consisting of a precursor of the coat proteins. The substitution mutation of Asp of the RTSV polyprotein had no effect on proteolysis; however, His, Glu, Cys and His proved to be essential for catalytic activity and could constitute the catalytic centre and/or substrate-binding pocket of the RTSV 3C-like protease.

  • Received:
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© Microbiology Society
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2002-12-01
2024-04-25
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Characterization of a protein from Rice tungro spherical virus with serine proteinase-like activity
J. Gen. Virol. 83, 3179 (2002); https://doi.org/10.1099/0022-1317-83-12-3179
/content/journal/jgv/10.1099/0022-1317-83-12-3179
/content/journal/jgv/10.1099/0022-1317-83-12-3179
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