The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide.
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.
Valente
Filipa M A
FM
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 1781-901 Oeiras, Portugal.
Pereira
Patrícia M
PM
Venceslau
Sofia S
SS
Regalla
Manuela
M
Coelho
Ana V
AV
Pereira
Inês A C
IA
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D017124:Conserved Sequence; D016969:Desulfovibrio vulgaris / Q000201:enzymology* / Q000235:genetics; D006864:Hydrogenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008074:Lipoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000235:genetics; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment
D008074:Lipoproteins; D021382:Protein Sorting Signals; D021122:Protein Subunits; C058560:nickel-iron-selenium hydrogenase; D006864:Hydrogenase