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 Lettjournal_title
FEBS lettersauthors
Dubini A,Sargent Fdoi
10.1016/s0014-5793(03)00802-0keywords:
subject
Has Abstractpub_date
2003-08-14 00:00:00pages
141-6issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579303008020journal_volume
549pub_type
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