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Assembly of Tat‐dependent [NiFe] hydrogenases: identification of precursor‐binding accessory proteins
Author(s) -
Dubini Alexandra,
Sargent Frank
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00802-0
Subject(s) - hydrogenase , protein subunit , cofactor , biochemistry , signal peptide , chemistry , escherichia coli , enzyme , peptide sequence , biology , gene
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.