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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Dubini A,Sargent F

doi

10.1016/s0014-5793(03)00802-0

keywords:

subject

Has Abstract

pub_date

2003-08-14 00:00:00

pages

141-6

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579303008020

journal_volume

549

pub_type

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