| Acylation of proteins of the archaebacteria Halobacterium cutirubrum and Methanobacterium thermoautotrophicum. | |
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MedLine Citation:
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PMID: 7986808 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Although the membrane lipids of extremely halophilic archaebacteria are exclusively derived from diphytanylglycerol diether, which is non-acylated, small amounts of fatty acids have been detected in these organisms. These fatty acids are formed by the action of a fatty acid synthase (FAS), shown to be present in the extreme halophile Halobacterium cutirubrum, despite the fact that only a fraction of the activity of FAS remains at the high salt concentration (> 4 M) present in the cytoplasm. It has now been demonstrated that fatty acids do not occur in lipid-bound form but largely in the form of acylated proteins in the red membrane of H. cutirubrum. In contrast, the bacteriorhodopsin of the purple membrane of this extreme halophile does not appear to be acylated. The thermophilic methanogen, Methanobacterium thermoautotrophicum had a much higher fatty acid synthase activity than the extreme halophile, and the synthase activity of the methanogen was optimal under its normal (anaerobic) growth conditions. The methanogen also utilized the resulting fatty acids to acylate its membrane proteins. The major fatty acids in both organisms were palmitic and stearic acids with small amounts of myristic and 18:1 acids, and these were bound to protein through both ester and amide linkages. |
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Authors:
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E L Pugh; M Kates |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1196 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1994 Nov |
Date Detail:
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Created Date: 1995-01-12 Completed Date: 1995-01-12 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 38-44 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, University of Ottawa, Ont., Canada. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acylation Bacterial Proteins / metabolism* Fatty Acid Synthetase Complex / metabolism Fatty Acids / analysis Halobacterium / metabolism* Membrane Lipids / chemistry Membrane Proteins / chemistry Methanobacterium / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Fatty Acids; 0/Membrane Lipids; 0/Membrane Proteins; EC 6.-/Fatty Acid Synthetase Complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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