期刊
FEBS LETTERS
卷 549, 期 1-3, 页码 141-146出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)00802-0
关键词
twin-arginine translocation protein transport; system; twin-arginine signal peptide; [NiFe] hydrogenase; accessory protein; Escherichia coli
The Escherichia coli twin-arginine translocation (Tat) system serves to export fully folded protein substrates across the bacterial cytoplasmic membrane. Respiratory [NiFe] hydrogenases are synthesised as precursors with twin-arginine signal peptides and transported as large, cofactor-containing, multi-subunit complexes by the Tat system. Cofactor insertion and assembly of [NiFe] hydrogenases requires coordination of networks of accessory proteins. In this work we utilise a bacterial two-hybrid assay to demonstrate protein-protein interactions between the uncharacterised chaperones HyaE and HybE with Tat signal peptide-bearing hydrogenase precursors. It is proposed that the chaperones act at a 'proofreading' stage in hydrogenase assembly and police the protein transport pathway preventing premature targeting of Tat-dependent hydrogenases. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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