Document Detail


The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis.
MedLine Citation:
PMID:  23281480     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Jan-Ulrik Dahl; Christin Radon; Martin Bühning; Manfred Nimtz; Lars I Leichert; Yann Denis; Cécile Jourlin-Castelli; Chantal Iobbi-Nivol; Vincent Méjean; Silke Leimkühler
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-01-01
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  288     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-02-25     Completed Date:  2013-04-25     Revised Date:  2014-02-25    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5426-42     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Carbon-Sulfur Lyases / metabolism
Coenzymes / biosynthesis*
Electrophoresis, Gel, Two-Dimensional
Escherichia coli / metabolism*
Escherichia coli Proteins / metabolism*
Gene Expression Regulation, Bacterial*
Iron-Sulfur Proteins / metabolism
Metalloproteins / biosynthesis*
Models, Biological
Mutation
Oligonucleotide Array Sequence Analysis / methods
Pteridines
RNA, Transfer / metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
Sulfhydryl Compounds / chemistry
Sulfides / chemistry
Sulfur / metabolism*
Surface Plasmon Resonance / methods
Transcription, Genetic
Chemical
Reg. No./Substance:
0/Coenzymes; 0/Escherichia coli Proteins; 0/Iron-Sulfur Proteins; 0/Metalloproteins; 0/Pteridines; 0/Sulfhydryl Compounds; 0/Sulfides; 0/TusA protein, E coli; 0/persulfides; 70FD1KFU70/Sulfur; 73508-07-3/molybdenum cofactor; 9014-25-9/RNA, Transfer; EC 4.4.-/Carbon-Sulfur Lyases; EC 4.4.1.-/cysteine desulfurase
Comments/Corrections

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