Journal Article

FZJ-2015-00291

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Subtilase SprP exerts pleiotropic effects in Pseudomonas aeruginosa

Pelzer, A. (Corresponding Author)FZJ* ; Polen, T.FZJ* ; Funken, H.FZJ* ; Rosenau, F. ; Wilhelm, S.FZJ* ; Bott, M.FZJ* ; Jaeger, K.-E.FZJ*

2014
Wiley Malden, Mass.

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Please use a persistent id in citations: http://hdl.handle.net/2128/8248  doi:10.1002/mbo3.150

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.

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Contributing Institute(s):

1. Institut für Molekulare Enzymtechnologie (HHUD) (IMET)
2. Biotechnologie (IBG-1)

Research Program(s):

1. 89581 - Biotechnology (POF2-89581) (POF2-89581)

Appears in the scientific report 2014

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Database coverage:
; ; ; ; BIOSIS Previews ; NCBI Molecular Biology Database ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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