UNSPECIFIED (2000) Sxa2 is a serine carboxypeptidase that degrades extracellular P-factor in the fission yeast Schizosaccharomyces pombe. MOLECULAR MICROBIOLOGY, 36 (2). pp. 377-390. ISSN 0950-382X

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Abstract

Stimulating the fission yeast Schizosaccharomyces pombe with mating pheromones brings about responses that lead to cell conjugation. Persistent stimulation does not, however, induce a continuous response as the cells become desensitized to the presence of the pheromone. One mechanism that contributes to desensitization in M-cells is the release of a carboxypeptidase that inactivates the extracellular P-factor pheromone. Production of the carboxypeptidase requires a functional sxa2 gene. In this study, we report the first molecular characterization of the Sxa2 protein and provide direct evidence that it is the carboxypeptidase that degrades P-factor. Sxa2 is synthesized as a precursor that undergoes an internal cleavage event catalysed by a protease with specificity for basic residues. This generates a series of catalytically active N-terminal fragments and an inactive C-terminal fragment. Cleavage is essential for activation of the carboxypeptidase and, although the C-terminal fragment is inactive, it is required for the N-terminal fragment to attain activity.

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:	April 2000
Volume:	36
Number:	2
Number of Pages:	14
Page Range:	pp. 377-390
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/13401

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