Subtilase SprP exerts pleiotropic effects in Pseudomonas aeruginosa

MicrobiologyOpen

Alexander Pelzer²  Tino Polen¹  Horst Funken²  Frank Rosenau³  Susanne Wilhelm²  Michael Bott¹ 

[1] Institut of Bio- und Geosciences IBG-1: Biotechnology, Research Centre Juelich, Juelich, Germany;Institute of Molecular Enzyme Technology, Research Centre Juelich, Heinrich-Heine-University Duesseldorf, Juelich, Germany;Institute of Pharmaceutical Biotechnology, Ulm-University, Ulm, Germany

关键词: Biofilm;    microarray;    motility;    orf PA1242;    protease;    Pseudomonas aeruginosa;    Pyoverdine.;   

DOI  :  10.1002/mbo3.150

来源: Wiley

【 摘 要 】

Abstract

The open reading frame PA1242 in the genome of Pseudomonas aeruginosa PAO1 encodes a putative protease belonging to the peptidase S8 family of subtilases. The respective enzyme termed SprP consists of an N-terminal signal peptide and a so-called S8 domain linked by a domain of unknown function (DUF). Presumably, this DUF domain defines a discrete class of Pseudomonas proteins as homologous domains can be identified almost exclusively in proteins of the genus Pseudomonas. The sprP gene was expressed in Escherichia coli and proteolytic activity was demonstrated. A P. aeruginosa ∆sprP mutant was constructed and its gene expression pattern compared to the wild-type strain by genome microarray analysis revealing altered expression levels of 218 genes. Apparently, SprP is involved in regulation of a variety of different cellular processes in P. aeruginosa including pyoverdine synthesis, denitrification, the formation of cell aggregates, and of biofilms.

【 授权许可】

CC BY   
© 2013 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.

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