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HtrA protease and processing of extracellular proteins of Streptococcus mutans

Lookup NU author(s): Emeritus Professor Roy Russell

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Abstract

A homologue of the HtrA family of stress-response proteases was detected by analysis of the Streptococcus mutans genome sequence. Disabling of the S. mutans htrA gene by insertional inactivation resulted in bacterial clumping in liquid medium, altered colony morphology and a reduced ability to withstand high temperature, extremes of pH or oxidative stress. Seven different extracellular or wall-associated proteins that are known to be subject to post-translational proteolysis were examined in cultures of wild-type S. mutans and an htrA mutant. Inactivation of the htrA protease had no effect on degradation of the proteins. © 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

Publication metadata

Author(s): Russell RRB; Diaz-Torres ML

Publication type: Article

Publication status: Published

Journal: FEMS Microbiology Letters

Year: 2001

Volume: 204

Issue: 1

Pages: 23-28

ISSN (print): 0378-1097

ISSN (electronic): 1574-6968

Publisher: Wiley-Blackwell

URL: http://dx.doi.org/10.1016/S0378-1097(01)00374-3

DOI: 10.1016/S0378-1097(01)00374-3

PubMed id: 11682172

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