Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/111880
Title: Expression and processing of human rhinovirus type 14 polypeptide precursors in Escherichia coli maxicells
Authors: Cheah, K.-C.
Sankar, S. 
Porter, A.G. 
Keywords: autoproteolysis
cDNA
picomavirus
plasmid
protease 3C
Recombinant DNA
trp promoter
zinc ions
Issue Date: 30-Sep-1988
Citation: Cheah, K.-C.,Sankar, S.,Porter, A.G. (1988-09-30). Expression and processing of human rhinovirus type 14 polypeptide precursors in Escherichia coli maxicells. Gene 69 (2) : 265-274. ScholarBank@NUS Repository.
Abstract: Human rhinovirus serotype-14 (HRV-14) cDNA, encompassing 87.9% of the coding region, was subcloned in an Escherichia coli expression vector, generating plasmid pKCC101. HRV-14 polypeptides encoded by pKCC101 were synthesized in E. coli maxicells. Pulse-chase experiments with pKCC110, a smaller derivative of pKCC101 containing the protease 3C coding region, have clearly demonstrated the proteolysis of a 55-kDa precursor to several polypeptides, including a doublet with the expected size of protease 3C (20 kDa). The proteolysis of the 55-kDa precursor polypeptide was prevented by ZnCl2, a known inhibitor of picornavirus 3C proteases. Results with a derivative of pKCC110 (pKCC115) which is partially deleted for the protease 3C sequence, support the idea that the doublet proteins are specified by the protease 3C coding region. Taken together, our investigations indicate that the precursor form of protease 3C must be responsible for its own cleavage. © 1988.
Source Title: Gene
URI: http://scholarbank.nus.edu.sg/handle/10635/111880
ISSN: 03781119
Appears in Collections:Staff Publications

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