Valente Filipa M A, Pereira Patrícia M, Venceslau Sofia S, Regalla Manuela, Coelho Ana V, Pereira Inês A C
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 1781-901 Oeiras, Portugal.
FEBS Lett. 2007 Jul 24;581(18):3341-4. doi: 10.1016/j.febslet.2007.06.020. Epub 2007 Jun 21.
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.
希登伯勒嗜硫还原菌拥有一种膜结合的[NiFeSe]氢化酶，由于它由两个亲水性亚基组成，其膜结合方式尚不清楚。这项研究表明，这种氢化酶是一种细菌脂蛋白，通过大亚基N端的脂质基团与膜结合，这很不寻常，因为它缺少典型的脂蛋白信号肽。然而，大亚基有一个保守的四残基脂盒，其合成对信号肽酶II抑制剂球霉素敏感。希登伯勒嗜硫还原菌的[NiFeSe]氢化酶是通过Tat途径转运的细菌脂蛋白的首个实例。
