Lipids activate SecA for high affinity binding to the SecYEG complex
| Autor: | Andreas Herrmann, Pavlo Gordiichuk, Janny G. de Wit, Iuliia Vos, Arnold J. M. Driessen, Jan Peter Birkner, Sabrina Koch, Antoine M. van Oijen |
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| Přispěvatelé: | Molecular Microbiology, Zernike Institute for Advanced Materials, Polymer Chemistry and Bioengineering, Nanotechnology and Biophysics in Medicine (NANOBIOMED) |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Lipid Bilayers Biology NANOLIPOPROTEIN PARTICLES Biochemistry environment and public health DEPENDENT MANNER 03 medical and health sciences Bacterial Proteins Heterotrimeric G protein Membrane Biology Escherichia coli Protein–lipid interaction PROTEIN-TRANSLOCATION PHOSPHOLIPID-BILAYER Lipid bilayer Molecular Biology Phospholipids IN-VIVO Adenosine Triphosphatases SecYEG Translocon SecA Proteins 030102 biochemistry & molecular biology Escherichia coli Proteins COLI PLASMA-MEMBRANE Cell Biology ACIDIC PHOSPHOLIPIDS Transport protein Protein Transport 030104 developmental biology Membrane protein complex ESCHERICHIA-COLI Biophysics bacteria ATPASE PREPROTEIN TRANSLOCASE lipids (amino acids peptides and proteins) Membrane biophysics SEC Translocation Channels |
| Zdroj: | The Journal of Biological Chemistry, 291(43), 22534-22543. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| ISSN: | 1083-351X 0021-9258 |
| DOI: | 10.1074/jbc.M116.743831 |
| Popis: | Protein translocation across the bacterial cytoplasmic membrane is an essential process catalyzed predominantly by the Sec translocase. This system consists of the membrane-embedded protein-conducting channel SecYEG, the motor ATPase SecA, and the heterotrimeric SecDFyajC membrane protein complex. Previous studies suggest that anionic lipids are essential for SecA activity and that the N-terminus of SecA is capable of penetrating the lipid bilayer. The role of lipid binding, however, has remained elusive. By employing differently sized nanodiscs reconstituted with single SecYEG complexes and comprising varying amounts of lipids, we establish that SecA gains access to the SecYEG complex via a lipid-bound intermediate state, whilst acidic phospholipids allosterically activate SecA for ATP-dependent protein translocation. |
| Databáze: | OpenAIRE |
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