In:
FEBS Letters, Wiley, Vol. 549, No. 1-3 ( 2003-08-14), p. 141-146
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(03)00802-0
Language:
English
Publisher:
Wiley
Publication Date:
2003
detail.hit.zdb_id:
212746-5
detail.hit.zdb_id:
1460391-3
SSG:
12
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