PMID:11438688
| Citation |
Xi, J, Ge, Y, Kinsland, C, McLafferty, FW and Begley, TP (2001) Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein--protein conjugate that is functionally analogous to the ubiquitin/E1 complex. Proc. Natl. Acad. Sci. U.S.A. 98:8513-8 |
|---|---|
| Abstract |
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 Escherichia coli thiF(-) using thiF(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. |
| Links |
PubMed PMC37467 Online version:10.1073/pnas.141226698 |
| Keywords |
Acylation; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Carrier Proteins; Cross-Linking Reagents; Disulfides; Escherichia coli/metabolism; Escherichia coli Proteins; Ligases/metabolism; Molecular Structure; Nucleotidyltransferases/chemistry; Nucleotidyltransferases/metabolism; Thiamine Pyrophosphate/biosynthesis; Thiamine Pyrophosphate/chemistry; Thiazoles/metabolism; Ubiquitin-Protein Ligases; Ubiquitins/metabolism |
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