Publication

Co-operation between different targeting pathways during integration of a membrane protein

Keller, R., de Keyzer, J., Driessen, A. J. M. & Palmer, T., 15-Oct-2012, In : Journal of Cell Biology. 199, 2, p. 303-315 13 p.

Research output: Contribution to journalArticleAcademicpeer-review

Membrane protein assembly is a fundamental process in all cells. The membrane-bound Rieske iron-sulfur protein is an essential component of the cytochrome bc(1) and cytochrome b(6)f complexes, and it is exported across the energy-coupling membranes of bacteria and plants in a folded conformation by the twin arginine protein transport pathway (Tat) transport pathway. Although the Rieske protein in most organisms is a monotopic membrane protein, in actinobacteria, it is a polytopic protein with three transmembrane domains. In this work, we show that the Rieske protein of Streptomyces coelicolor requires both the Sec and the Tat pathways for its assembly. Genetic and biochemical approaches revealed that the initial two transmembrane domains were integrated into the membrane in a Sec-dependent manner, whereas integration of the third transmembrane domain, and thus the correct orientation of the iron-sulfur domain, required the activity of the Tat translocase. This work reveals an unprecedented co-operation between the mechanistically distinct Sec and Tat systems in the assembly of a single integral membrane protein.

Original languageEnglish
Pages (from-to)303-315
Number of pages13
JournalJournal of Cell Biology
Volume199
Issue number2
Publication statusPublished - 15-Oct-2012

    Keywords

  • TWIN-ARGININE TRANSLOCASE, MALTOSE-BINDING PROTEIN, DIHEME CYTOCHROME C(1), RIESKE FE/S PROTEIN, ESCHERICHIA-COLI, CYTOPLASMIC MEMBRANE, CORYNEBACTERIUM-GLUTAMICUM, EXPORT PATHWAY, YIDC, TRANSPORT

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