3C-like protease encoded by Rice tungro spherical virus is autocatalytically processed

3C-like protease encoded by Rice tungro spherical virus is autocatalytically processed The 3C-protease of Rice tungro spherical virus (RTSV) was previously identified as a cis - and trans -acting protease. In vitro translation of the protease resulted in several protein products, demonstrating that the protease is cleaved by itself. The protease was then produced in Escherichia coli as a fusion protein with maltose-binding protein (MBP). Two forms of the protease were purified after MBP affinity chromatography in the column buffer. After analyses of the purified proteins, we speculated that a major internal cleavage site was in the C-terminal half. A point mutation was introduced at a potential major self-cleavage site (C 2763 ). The mutation abolished the catalytic activity, suggesting that the mutation site is important for the recognition of the protease. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

3C-like protease encoded by Rice tungro spherical virus is autocatalytically processed

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Publisher
Springer-Verlag
Copyright
Copyright © 2005 by Springer-Verlag/Wien
Subject
Biomedicine; Medical Microbiology; Virology; Infectious Diseases
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-004-0421-9
Publisher site
See Article on Publisher Site

Abstract

The 3C-protease of Rice tungro spherical virus (RTSV) was previously identified as a cis - and trans -acting protease. In vitro translation of the protease resulted in several protein products, demonstrating that the protease is cleaved by itself. The protease was then produced in Escherichia coli as a fusion protein with maltose-binding protein (MBP). Two forms of the protease were purified after MBP affinity chromatography in the column buffer. After analyses of the purified proteins, we speculated that a major internal cleavage site was in the C-terminal half. A point mutation was introduced at a potential major self-cleavage site (C 2763 ). The mutation abolished the catalytic activity, suggesting that the mutation site is important for the recognition of the protease.

Journal

Archives of VirologySpringer Journals

Published: Mar 1, 2005

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