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Archives of Microbiology

, Volume 173, Issue 5–6, pp 319–324 | Cite as

Membrane targeting and translocation of bacterial hydrogenases

  • Long-Fei Wu
  • Angélique Chanal
  • Agnès Rodrigue
Mini-Review

Abstract.

Periplasmic or membrane-bound bacterial hydrogenases are generally composed of a small subunit and a large subunit. The small subunit contains a peculiar N-terminal twin-arginine signal peptide, whereas the large subunit lacks any known targeting signal for export. Genetic and biochemistry data support the assumption that the large subunit is cotranslocated with the small subunit across the cytoplasmic membrane. Indeed, the signal peptide carried by the small subunit directs both the small and the large subunits to the recently identified Mtt/Tat pathway, independently of the Sec machinery. In addition, the twin-arginine signal peptide of hydrogenase is capable of directing protein import into the thylakoidal lumen of chloroplasts via the homologous ΔpH-driven pathway, which is independent of the Sec machinery. Therefore, the translocation of hydrogenase shares characteristics with the ΔpH-driven import pathway in terms of Sec-independence and requirement for the twin-arginine signal peptide, and with protein import into peroxisomes in a "piggyback" fashion.

Hydrogenase Metalloenzyme Folding Enzyme complex Signal peptide Twin-arginine Membrane targeting Cotranslocation Sec system Mtt/Tat system 

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Copyright information

© Springer-Verlag 2000

Authors and Affiliations

  • Long-Fei Wu
    • 1
  • Angélique Chanal
    • 1
  • Agnès Rodrigue
    • 2
  1. 1.Laboratoire de Chimie Bactérienne, UPR9043 CNRS, Institut de Biologie Structurale et Microbiologie, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, FranceFrance
  2. 2.Unité de Microbiologie et Génétique, UMR5577 CNRS, Institut National des Sciences Appliquées, Bât. 406, 20 av. A. Einstein, 69621 Villeurbanne cedex, FranceFrance

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