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PsrR, a member of the AraC family of transcriptional regulators, is required for the synthesis of Wolinella succinogenes polysulfide reductase.

Braatsch, S. and Krafft, T. and Simon, J. and Gross, R. and Klimmek, O. and Kröger, A. (2002):
PsrR, a member of the AraC family of transcriptional regulators, is required for the synthesis of Wolinella succinogenes polysulfide reductase.
In: Archives of microbiology, pp. 202-7, 178, (3), ISSN 0302-8933, [Article]

Abstract

Wolinella succinogenes grows by polysulfide respiration with formate or hydrogen as electron donor. Polysulfide reduction is catalyzed by the membrane-bound polysulfide reductase complex encoded by the psrABC operon. An open reading frame, designated psrR, was found in close proximity upstream of the psr operon, but oriented in the opposite direction. The deduced amino acid sequence of PsrR is similar to those of transcriptional regulators of the AraC family and includes all typical features. Polysulfide reductase is not detectable in a Delta psrR deletion mutant of W. succinogenes. Mutant cells grown with fumarate as terminal electron acceptor did not catalyze polysulfide reduction with formate or hydrogen, in contrast to the wild-type strain. The phenotype of W. succinogenes wild-type cells was restored by genomic complementation of W. succinogenes Delta psrR. The results suggest that the gene product of psrR is involved in the regulation of polysulfide reductase synthesis.

Item Type: Article
Erschienen: 2002
Creators: Braatsch, S. and Krafft, T. and Simon, J. and Gross, R. and Klimmek, O. and Kröger, A.
Title: PsrR, a member of the AraC family of transcriptional regulators, is required for the synthesis of Wolinella succinogenes polysulfide reductase.
Language: English
Abstract:

Wolinella succinogenes grows by polysulfide respiration with formate or hydrogen as electron donor. Polysulfide reduction is catalyzed by the membrane-bound polysulfide reductase complex encoded by the psrABC operon. An open reading frame, designated psrR, was found in close proximity upstream of the psr operon, but oriented in the opposite direction. The deduced amino acid sequence of PsrR is similar to those of transcriptional regulators of the AraC family and includes all typical features. Polysulfide reductase is not detectable in a Delta psrR deletion mutant of W. succinogenes. Mutant cells grown with fumarate as terminal electron acceptor did not catalyze polysulfide reduction with formate or hydrogen, in contrast to the wild-type strain. The phenotype of W. succinogenes wild-type cells was restored by genomic complementation of W. succinogenes Delta psrR. The results suggest that the gene product of psrR is involved in the regulation of polysulfide reductase synthesis.

Journal or Publication Title: Archives of microbiology
Volume: 178
Number: 3
Divisions: 10 Department of Biology > Microbial Energy Conversion and Biotechnology
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10 Department of Biology
Date Deposited: 07 Dec 2010 15:17
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