The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis.

2.50
Hdl Handle:
http://hdl.handle.net/10033/291142
Title:
The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis.
Authors:
Dahl, Jan-Ulrik; Radon, Christin; Bühning, Martin; Nimtz, Manfred; Leichert, Lars I; Denis, Yann; Jourlin-Castelli, Cécile; Iobbi-Nivol, Chantal; Méjean, Vincent; Leimkühler, Silke
Abstract:
The Escherichia coli L-cysteine desulfurase IscS mobilizes sulfur from L-cysteine for the synthesis of several biomolecules such as iron-sulfur (FeS) clusters, molybdopterin, thiamin, lipoic acid, biotin, and the thiolation of tRNAs. The sulfur transfer from IscS to various biomolecules is mediated by different interaction partners (e.g. TusA for thiomodification of tRNAs, IscU for FeS cluster biogenesis, and ThiI for thiamine biosynthesis/tRNA thiolation), which bind at different sites of IscS. Transcriptomic and proteomic studies of a ΔtusA strain showed that the expression of genes of the moaABCDE operon coding for proteins involved in molybdenum cofactor biosynthesis is increased under aerobic and anaerobic conditions. Additionally, under anaerobic conditions the expression of genes encoding hydrogenase 3 and several molybdoenzymes such as nitrate reductase were also increased. On the contrary, the activity of all molydoenzymes analyzed was significantly reduced in the ΔtusA mutant. Characterization of the ΔtusA strain under aerobic conditions showed an overall low molybdopterin content and an accumulation of cyclic pyranopterin monophosphate. Under anaerobic conditions the activity of nitrate reductase was reduced by only 50%, showing that TusA is not essential for molybdenum cofactor biosynthesis. We present a model in which we propose that the direction of sulfur transfer for each sulfur-containing biomolecule is regulated by the availability of the interaction partner of IscS. We propose that in the absence of TusA, more IscS is available for FeS cluster biosynthesis and that the overproduction of FeS clusters leads to a modified expression of several genes.
Affiliation:
Institute of Biochemistry and Biology, Department of Molecular Enzymology, University of Potsdam, 14476 Potsdam, Germany.
Citation:
The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis. 2013, 288 (8):5426-42 J. Biol. Chem.
Journal:
The Journal of biological chemistry
Issue Date:
22-Feb-2013
URI:
http://hdl.handle.net/10033/291142
DOI:
10.1074/jbc.M112.431569
PubMed ID:
23281480
Type:
Article
Language:
en
ISSN:
1083-351X
Appears in Collections:
publications of the research group cellular proteom research (CPRO)

Full metadata record

DC FieldValue Language
dc.contributor.authorDahl, Jan-Ulriken_GB
dc.contributor.authorRadon, Christinen_GB
dc.contributor.authorBühning, Martinen_GB
dc.contributor.authorNimtz, Manfreden_GB
dc.contributor.authorLeichert, Lars Ien_GB
dc.contributor.authorDenis, Yannen_GB
dc.contributor.authorJourlin-Castelli, Cécileen_GB
dc.contributor.authorIobbi-Nivol, Chantalen_GB
dc.contributor.authorMéjean, Vincenten_GB
dc.contributor.authorLeimkühler, Silkeen_GB
dc.date.accessioned2013-05-15T14:08:50Z-
dc.date.available2013-05-15T14:08:50Z-
dc.date.issued2013-02-22-
dc.identifier.citationThe sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis. 2013, 288 (8):5426-42 J. Biol. Chem.en_GB
dc.identifier.issn1083-351X-
dc.identifier.pmid23281480-
dc.identifier.doi10.1074/jbc.M112.431569-
dc.identifier.urihttp://hdl.handle.net/10033/291142-
dc.description.abstractThe Escherichia coli L-cysteine desulfurase IscS mobilizes sulfur from L-cysteine for the synthesis of several biomolecules such as iron-sulfur (FeS) clusters, molybdopterin, thiamin, lipoic acid, biotin, and the thiolation of tRNAs. The sulfur transfer from IscS to various biomolecules is mediated by different interaction partners (e.g. TusA for thiomodification of tRNAs, IscU for FeS cluster biogenesis, and ThiI for thiamine biosynthesis/tRNA thiolation), which bind at different sites of IscS. Transcriptomic and proteomic studies of a ΔtusA strain showed that the expression of genes of the moaABCDE operon coding for proteins involved in molybdenum cofactor biosynthesis is increased under aerobic and anaerobic conditions. Additionally, under anaerobic conditions the expression of genes encoding hydrogenase 3 and several molybdoenzymes such as nitrate reductase were also increased. On the contrary, the activity of all molydoenzymes analyzed was significantly reduced in the ΔtusA mutant. Characterization of the ΔtusA strain under aerobic conditions showed an overall low molybdopterin content and an accumulation of cyclic pyranopterin monophosphate. Under anaerobic conditions the activity of nitrate reductase was reduced by only 50%, showing that TusA is not essential for molybdenum cofactor biosynthesis. We present a model in which we propose that the direction of sulfur transfer for each sulfur-containing biomolecule is regulated by the availability of the interaction partner of IscS. We propose that in the absence of TusA, more IscS is available for FeS cluster biosynthesis and that the overproduction of FeS clusters leads to a modified expression of several genes.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to The Journal of biological chemistryen_GB
dc.subject.meshCarbon-Sulfur Lyasesen_GB
dc.subject.meshCoenzymesen_GB
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_GB
dc.subject.meshEscherichia colien_GB
dc.subject.meshEscherichia coli Proteinsen_GB
dc.subject.meshGene Expression Regulation, Bacterialen_GB
dc.subject.meshIron-Sulfur Proteinsen_GB
dc.subject.meshMetalloproteinsen_GB
dc.subject.meshModels, Biologicalen_GB
dc.subject.meshMutationen_GB
dc.subject.meshOligonucleotide Array Sequence Analysisen_GB
dc.subject.meshPteridinesen_GB
dc.subject.meshRNA, Transferen_GB
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen_GB
dc.subject.meshSulfhydryl Compoundsen_GB
dc.subject.meshSulfidesen_GB
dc.subject.meshSulfuren_GB
dc.subject.meshSurface Plasmon Resonanceen_GB
dc.subject.meshTranscription, Geneticen_GB
dc.titleThe sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis.en
dc.typeArticleen
dc.contributor.departmentInstitute of Biochemistry and Biology, Department of Molecular Enzymology, University of Potsdam, 14476 Potsdam, Germany.en_GB
dc.identifier.journalThe Journal of biological chemistryen_GB

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