Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally...

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Bibliographische Detailangaben
Zeitschriftentitel:	Proceedings of the National Academy of Sciences
Personen und Körperschaften:	Xi, Jun, Ge, Ying, Kinsland, Cynthia, McLafferty, Fred W., Begley, Tadhg P.
In:	Proceedings of the National Academy of Sciences, 98, 2001, 15, S. 8513-8518
Format:	E-Article
Sprache:	Englisch
veröffentlicht:	Proceedings of the National Academy of Sciences
Schlagwörter:	Multidisciplinary

Details
Zusammenfassung:	<jats:p> A covalently linked protein–protein conjugate between ThiF and ThiS thiocarboxylate was found in a partially purified coexpressed ThiF/ThiS protein mixture by using Fourier transform mass spectrometry. The Cys-184 of ThiF and the C terminus of ThiS thiocarboxylate were identified to be involved in the formation of this complex by using both mutagenesis and chemical modification methods. A complementation study of <jats:italic> Escherichia coli thiF <jats:sup>−</jats:sup> </jats:italic> using <jats:italic>thiF</jats:italic> (C184S) suggests that this conjugate is an essential intermediate involved in the biosynthesis of the thiazole moiety of thiamin. This ThiF/ThiS conjugate is the first characterized example of a unique acyldisulfide intermediate in a biosynthetic system. This protein conjugate is also an example of an ubiquitin-E1 like protein–protein conjugate in prokaryotes and supports a strong evolutionary link between thiamin biosynthesis and the ubiquitin conjugating system. </jats:p>
Umfang:	8513-8518
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.141226698