White Rose University Consortium logo
University of Leeds logo University of Sheffield logo York University logo

The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions

Brannigan, J.A., Hoa, N.T. and Cutting, S.M. (2001) The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions. Journal of Bacteriology. pp. 4364-4373. ISSN 0021-9193

Full text available as:
[img]
Preview
Text (branniganja3.pdf)
branniganja3.pdf

Download (1909Kb)

Abstract

During spore formation in Bacillus subtilis, the SpoIVB protein is a critical component of the sigma (K) regulatory checkpoint. SpoIVB has been shown to be a serine peptidase that is synthesized in the spore chamber and which self-cleaves, releasing active forms. These forms can signal proteolytic processing of the transcription factor sigma (K) in the outer mother cell chamber of the sporulating cell. This forms the basis of the sigma (K) checkpoint and ensures accurate sigma (K)-controlled gene expression. SpoIVB has also been shown to activate a second distinct process, termed the second function, which is essential for the formation of heat-resistant spores. In addition to the serine peptidase domain, SpoIVB contains a PDZ domain. We have altered a number of conserved residues in the PDZ domain by site-directed mutagenesis and assayed the sporulation phenotype and signaling properties of mutant SpoIVB proteins. Our work has revealed that the SpoIVB PDZ domain could be used for up to four distinct processes, (i) targeting of itself for trans proteolysis, (11) binding to the protease inhibitor BofC, (iii) signaling of pro-sigma (K) processing, and (iv) signaling of the second function of SpoIVB.

Item Type: Article
Copyright, Publisher and Additional Information: Copyright © 2001 American Society for Microbiology
Keywords: DEVELOPMENTAL TRANSCRIPTION FACTOR, BACILLUS-SUBTILIS, GENE-EXPRESSION, MOTHER-CELL, PROTEOLYTIC ACTIVATION, SPORE FORMATION, PRO-SIGMA(K), RECOGNITION, SPORULATION, PROTEINS
Academic Units: The University of York > Chemistry (York)
Depositing User: Sherpa Assistant
Date Deposited: 04 Mar 2005
Last Modified: 17 Oct 2013 14:37
Published Version: http://dx.doi.org/10.1128/JB.183.14.4364-4373.2001
Status: Published
Refereed: Yes
URI: http://eprints.whiterose.ac.uk/id/eprint/314

Actions (login required)

View Item View Item