The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide |
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Authors: | Valente Filipa M A Pereira Patrícia M Venceslau Sofia S Regalla Manuela Coelho Ana V Pereira Inês A C |
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Institution: | Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 1781-901 Oeiras, Portugal. |
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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. |
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Keywords: | Lipoprotein Hydrogenase Tat pathway Signal peptidase II Desulfovibrio |
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