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

Alexandra Dubini, Frank Sargent

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76 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)141-146
Number of pages6
JournalFEBS Letters
Issue number1-3
Publication statusPublished - 14 Aug 2003

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