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

FEBS Letters

Sargent, Frank¹  Dubini, Alexandra¹ 

[1] Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK

关键词: Twin-arginine translocation protein transport system;    Twin-arginine signal peptide;    [NiFe] hydrogenase;    Accessory protein;    Escherichia coli;   

DOI  :  10.1016/S0014-5793(03)00802-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown