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.
Sekiguchi
H
H
Pathogen-Plant Interactions Group, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan.
Isogai
M
M
Masuta
C
C
Uyeda
I
I
D000086042:3C Viral Proteases; D001665:Binding Sites / Q000235:genetics; D002352:Carrier Proteins / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D058619:Maltose-Binding Proteins; D012275:Oryza / Q000821:virology*; D014176:Protein Biosynthesis; D011994:Recombinant Proteins / Q000096:biosynthesis; D014158:Transcription, Genetic; D014764:Viral Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D019193:Waikavirus / Q000201:enzymology*
D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D011994:Recombinant Proteins; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases