Non-bilayer lipids stimulate the activity of the reconstituted bacterial protein translocase
| Autor: | C. van der Does, W. van Klompenburg, Arnold J. M. Driessen, J Swaving |
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| Přispěvatelé: | GBB Cluster Microbiologie, Moleculaire Microbiologie, Groningen Biomolecular Sciences and Biotechnology |
| Jazyk: | Dutch; Flemish |
| Rok vydání: | 2000 |
| Předmět: |
Phospholipid
Biochemistry BACILLUS-SUBTILIS chemistry.chemical_compound SECA PROTEIN Bacterial Proteins Escherichia coli Translocase SIGNAL SEQUENCE Molecular Biology GeneralLiterature_REFERENCE(e.g. dictionaries encyclopedias glossaries) Phospholipids Adenosine Triphosphatases Phosphatidylethanolamine SecYEG Translocon Liposome SecA Proteins COLI PREPROTEIN TRANSLOCASE biology ANIONIC PHOSPHOLIPIDS Membrane transport protein Escherichia coli Proteins Bilayer PRECURSOR PROTEIN Membrane Transport Proteins Cell Biology ACIDIC PHOSPHOLIPIDS Enzyme Activation chemistry ESCHERICHIA-COLI biology.protein ComputingMethodologies_DOCUMENTANDTEXTPROCESSING lipids (amino acids peptides and proteins) NEGATIVELY CHARGED PHOSPHOLIPIDS Carrier Proteins SEC Translocation Channels MEMBRANE-VESICLES |
| Zdroj: | The Journal of Biological Chemistry, 275(4), 2472-2478. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| ISSN: | 0021-9258 |
| Popis: | To determine the phospholipid requirement of the preprotein translocase in vitro, the Escherichia coli SecYEG complex was purified in a delipidated form using the detergent dodecyl maltoside. SecYEG was reconstituted into liposomes composed of defined synthetic phospholipids, and proteoliposomes were analyzed for their preprotein translocation and SecA translocation ATPase activity. The activity strictly required the presence of anionic phospholipids, whereas the non-bilayer lipid phosphatidylethanolamine was found stimulatory. The latter effect could also be induced by dioleoylglycerol, a lipid that adopts a non-bilayer conformation. Phosphatidylethanolamine derivatives that prefer the bilayer state were unable to stimulate translocation. In the absence of SecG, activity was reduced, but the phospholipid requirement was unaltered. Remarkably, non-bilayer lipids were found essential for the activity of the Bacillus subtilis SecYEG complex. Optimal activity required a mixture of anionic and non-bilayer lipids at concentrations that correspond to concentrations found in the natural membrane. |
| Databáze: | OpenAIRE |
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