TAILIEUCHUNG - Báo cáo khoa học: The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin-arginine translocase

The Rieske [2Fe)2S] protein (ISP) is an essential subunit of cyto-chromebc1 complexes in mitochondrial and bacterial respiratory chains. Based on the presence of two consecutive arginines, it was argued that the ISP ofParacoccus denitrificans, a Gram-negative soil bacterium, is inserted into the cytoplasmic membrane via the twin-arginine translocation (Tat) pathway. | ỊFEBS Journal The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin-arginine translocase Julie Bachmann1 Brigitte Bauer1 Klaus Zwicker2 Bernd Ludwig1 and Oliver Anderka1 x 1 Institut fur Biochemie Johann Wolfgang Goethe-Universitat Frankfurt Germany 2 Zentrum der Biologischen Chemie Institut fur Molekulare Bioenergetik Universitats-Klinikum Frankfurt Germany Keywords cytochrome bc1 complex membrane targeting Paracoccus denitrificans Rieske iron-sulfur protein twin-arginine translocation Correspondence O. Anderka Institut fur Biochemie Johann Wolfgang Goethe-Universitat D-60438 Frankfurt Germany Fax 49 69 3058 1901 Tel 49 69 3051 2418 E-mail Present address Sanofi-aventis TD Metabolism Frankfurt Germany Received 16 June 2006 revised 23 August 2006 accepted 24 August 2006 doi The Rieske 2Fe-2S protein ISP is an essential subunit of cytochrome bc1 complexes in mitochondrial and bacterial respiratory chains. Based on the presence of two consecutive arginines it was argued that the ISP of Paracoccus denitrificans a Gram-negative soil bacterium is inserted into the cytoplasmic membrane via the twin-arginine translocation Tat pathway. Here we provide experimental evidence that membrane integration of the bacterial ISP indeed relies on the Tat translocon. We show that targeting of the ISP depends on the twin-arginine motif. A strict requirement is established particularly for the second arginine residue R16 conservative replacement of the first arginine R15K still permits substantial ISP transport. Comparative sequence analysis reveals characteristics common to Tat signal peptides in several bacterial ISPs however there are distinctive features relating to the fact that the presumed ISP Tat signal simultaneously serves as a membrane anchor. These differences include an elevated hydrophobicity of the h-region compared with generic Tat signals and the absence .

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