UNSPECIFIED (2000) A temperature-sensitive Krp1 allows in vivo characterization of kexin activation. MOLECULAR MICROBIOLOGY, 37 (3). pp. 606-618. ISSN 0950-382X

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Abstract

Members of the kexin family of processing enzymes are responsible for the cleavage of many proproteins during their transport through the secretory pathway. The enzymes are themselves made as inactive precursors and we have investigated the activation of Krp1, a kexin from the fission yeast Schizosaccharomyces pombe. As Krp1 is essential for cell growth, we have used a krp1(ts) strain to investigate the role of the prosequence in the activation process. Mutations that reduce either the efficiency with which the prosequence is released or the rate at which the released prosegment is subsequently cleaved at an internal site are less active when assayed in vivo. We also show that prosegments lacking an internal dibasic motif can act as autoinhibitors and prevent activation of the catalytic fragment. Krp1 constructs containing prosequences based on these inhibitors do not become active in vitro. Surprisingly, the same constructs do become active in the intact cell and appear to suggest that alternative activation processes can be used by these enzymes.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QR Microbiology
Journal or Publication Title:	MOLECULAR MICROBIOLOGY
Publisher:	BLACKWELL SCIENCE LTD
ISSN:	0950-382X
Date:	August 2000
Volume:	37
Number:	3
Number of Pages:	13
Page Range:	pp. 606-618
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/13067

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