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Article

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

The Journal of biological chemistry - 22 Feb 2013

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 excerpt

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...

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Identifiers

PMID: 23281480
DOI: 10.1074/jbc.M112.431569
PMCID: PMC3581435

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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