Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria.

Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria. Research Abstract Details 

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Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria. Abstract Text:

Thijs R H M Kouwen,Annemieke van der Goot,Ronald Dorenbos,Theresa Winter,Haike Antelmann,Marie-Claire Plaisier,Wim J Quax,January Maarten van Dijl,Jean-Yves F Dubois,

Disulphide bond formation catalysed by thiol-disulphide oxidoreductases (TDORs) is a universally conserved mechanism for stabilizing extracytoplasmic proteins. In Escherichia coli, disulphide bond formation requires a concerted action of distinct TDORs in thiol oxidation and subsequent quinone reduction. TDOR function in other bacteria has remained largely unexplored. Here we focus on TDORs of low-GC Gram-positive bacteria, in particular DsbA of Staphylococcus aureus and BdbA-D of Bacillus subtilis. Phylogenetic analyses reveal that the homologues DsbA and BdbD cluster in distinct groups typical for Staphylococcus and Bacillus species respectively. To compare the function of these TDORs, DsbA was produced in various bdb mutants of B. subtilis. Next, we assessed the ability of DsbA to sustain different TDOR-dependent processes, including heterologous secretion of E. coli PhoA, competence development and bacteriocin (sublancin 168) production. The results show that DsbA can function in all three processes. While BdbD needs a quinone oxidoreductase for activity, DsbA activity appears to depend on redox-active medium components. Unexpectedly, both quinone oxidoreductases of B. subtilis are sufficient to sustain production of sublancin. Moreover, DsbA can functionally replace these quinone oxidoreductases in sublancin production. Taken together, our unprecedented findings imply that TDOR systems of low-GC Gram-positive bacteria have a modular composition.

Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria. Publishing Authors By Initials

TR Kouwen,A van der Goot,R Dorenbos,T Winter,H Antelmann,MC Plaisier,WJ Quax,JM van Dijl,JY Dubois,

For similar bacteria: gram-positive bacteria: gram-positive cocci: staphylococcaceae: staphylococcus: staphylococcus aureus research abstracts see: bacteria: gram-positive bacteria: gram-positive cocci: staphylococcaceae: staphylococcus: staphylococcus aureus research

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Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular microbiology

VOLUME: 64

Page Numbers: 984-99

Journal Abbreviation: Mol. Microbiol.

ISSN: 0950-382X

DAY: 4

MONTH: May

YEAR: 2007

Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8712028

Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria. Keywords Mesh Terms:

KEYWORDS: Staphylococcus aureus

MESH TERMS: metabolism

Chemical & Substance for Abstract: Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria. Information

Substance Name: Protein Disulfide-Isomerase

Registry Number: EC 5.3.4.1

Grant and Affiliation Information for Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria.

AFFILIATION: Department of Medical Microbiology, University Medical Center Groningen and University of Groningen, Hanzeplein 1, PO Box 30001, 9700 RB Groningen, The Netherlands.

Country: England

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MEDLINETA: Mol Microbiol

REFSOURCE: Mol Microbiol. 2007 Jun;64(5):1417

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