Kueper, Ulf and Meyer, Carolin and Mueller, Volker and Rachel, Reinhard and Huber, Harald (2010) Energized outer membrane and spatial separation of metabolic processes in the hyperthermophilic Archaeon Ignicoccus hospitalis. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 107 (7). pp. 3152-3156. ISSN 0027-8424,
Full text not available from this repository. (Request a copy)Abstract
ATP synthase catalyzes ATP synthesis at the expense of an electrochemical ion gradient across a membrane that can be generated by different exergonic reactions. Sulfur reduction is the main energy-yielding reaction in the hyperthermophilic strictly anaerobic Crenarchaeon Ignicoccus hospitalis. This organism is unusual in having an inner and an outer membrane that are separated by a huge intermembrane-compartment. Here we show, on the basis of immuno-EM analyses of ultrathin sections and immunofluorescence experiments with whole I. hospitalis cells, that the ATP synthase and H-2:sulfur oxidoreductase complexes of this organism are located in the outer membrane. These two enzyme complexes are mandatory for the generation of an electrochemical gradient and for ATP synthesis. Thus, among all prokaryotes possessing two membranes in their cell envelope (including Planctomycetes, Gram-negative bacteria), I. hospitalis is a unique organism, with an energized outermembrane and ATP synthesis within the periplasmic space. In addition, DAPI staining and EM analyses showed that DNA and ribosomes are localized in the cytoplasm, leading to the conclusion that in I. hospitalis energy conservation is separated from information processing and protein biosynthesis. This raises questions regarding the function of the two membranes, the interaction between these compartments, and the general definition of a cytoplasmic membrane.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | A(1)A(0) ATP SYNTHASE; NANOARCHAEUM-EQUITANS; PYROCOCCUS-FURIOSUS; SP-NOV; TRANSPORT; INSIGHTS; ULTRASTRUCTURE; COMPLEXES; PROTEINS; ORIGIN; Archaea; ATP synthase; ATPase; immunolabeling; sulfur reductase |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) > Prof. Dr. Reinhard Rachel |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 06 Aug 2020 07:02 |
| Last Modified: | 06 Aug 2020 07:02 |
| URI: | https://pred.uni-regensburg.de/id/eprint/25147 |
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