Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins

Dubini, Alexandra and Sargent, Frank (2003) Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins. FEBS Letters, 549 (1-3). pp. 141-146. ISSN 1873-3468

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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.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Depositing User: LivePure Connector
Date Deposited: 12 Feb 2020 03:00
Last Modified: 21 Apr 2020 20:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/74133
DOI: 10.1016/S0014-5793(03)00802-0

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