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Translocation of precytochrome C 2 into intracytoplasmic membrane vesicles of Rhodobacter capsulatus requires a peripheral membrane protein
Author(s) -
Wieseler Beate,
Müller Matthias
Publication year - 1993
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1993.tb01108.x
Subject(s) - rhodobacter , biology , vesicle , membrane protein , rhodospirillaceae , peripheral membrane protein , biochemistry , bacteria , microbiology and biotechnology , membrane , bacterial outer membrane , cell membrane , chromosomal translocation , protein–lipid interaction , integral membrane protein , genetics , escherichia coli , mutant , gene
Summary Rhodobacter capsulatus is a member of the group α‐purple bacteria which are closely related to the ancestral endosymbiont that gave rise to mitochondria. It has therefore been hypothesized that the molecular mechanisms governing protein export in α‐purple bacteria have been conserved during the evolution of mitochondria. To enable analysis of protein export in α‐purple bacteria we describe here the development of a homologous cell‐free synthesis/export system consisting entirely of components of R. capsulatus. Translocation of precytochrome C 2 into intracytoplasmic membrane vesicles of this organism was found to require the proton‐motive force and proceed at a significantly higher efficiency when membranes were present during protein synthesis. Furthermore, we show that, in this cell‐free system, translocation depends on a preparation of peripheral membrane proteins Which do not possess detectable SecA‐ and SecB‐like actvities.