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Translocation of precytochrome C2 into intracytoplasmic membrane vesicles of Rhodobacter capsulatus requires a peripheral membrane protein (1993)

Wieseler, Beate ; Müller, Matthias

Oxford, UK : Blackwell Publishing Ltd

Molecular microbiology 7 (1993), S. 0

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ISSN: 1365-2958

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology , Medicine

Notes: 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 C2 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01108.x

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Oxygen tension regulated expression of the hemA gene of Rhodobacter capsulatus (1991)

Hornberger, Ulrike ; Wieseler, Beate ; Drews, Gerhart

Springer

Archives of microbiology 156 (1991), S. 129-134

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ISSN: 1432-072X

Keywords: δ-Aminolevulinic acid synthase ; Bacteriochlorophyll ; Promoter activity ; Oxygen regulation ; Rhodobacter capsulatus

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The promoter of the Rhodobacter capsulatus hemA gene, coding for the enzyme δ-aminolevulinic acid synthase (ALAS), was identified by trans-complementation of a δ-aminolevulinic acid (ALA)-dependent mutant and found to be located within a 170 bp region proximal to the hemA gene. The activity of the hemA promoter was demonstrated by lacZ fusion and in vitro transcription-translation. An open reading frame (ORFX) was found downstream of hemA. The activity of the hemA promoter, but not that of the ORFX promoter, increased when oxygen tension was lowered in the culture. Deletions upstream of the hemA promoter region did not affect ALAS activity and formation of pigment-protein complexes in R. capsulatus.