The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide

Filipa M.A. Valente, Patrícia M. Pereira, Sofia S. Venceslau, Manuela Regalla, Ana V. Coelho, Inês A.C. Pereira

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Desulfovibrio vulgaris Hildenborough has a membrane-bound [NiFeSe] hydrogenase whose mode of membrane association was unknown since it is constituted by two hydrophilic subunits. This work shows that this hydrogenase is a bacterial lipoprotein bound to the membrane by lipidic groups found at the N-terminus of the large subunit, which is unusual since it is missing the typical lipoprotein signal peptide. Nevertheless, the large subunit has a conserved four residue lipobox and its synthesis is sensitive to the signal peptidase II inhibitor globomycin. The D. vulgaris [NiFeSe] hydrogenase is the first example of a bacterial lipoprotein translocated through the Tat pathway.

Original languageEnglish
Pages (from-to)3341-3344
Number of pages4
JournalFEBS Letters
Volume581
Issue number18
DOIs
Publication statusPublished - 24 Jul 2007

    Fingerprint

Keywords

  • Desulfovibrio
  • Hydrogenase
  • Lipoprotein
  • Signal peptidase II
  • Tat pathway

Cite this