Arginine 357 of SecY is needed for SecA-dependent initiation of preprotein translocation
| Autor: | Arnold J. M. Driessen, Anouk Regeling, Jeanine de Keyzer |
|---|---|
| Přispěvatelé: | Molecular Microbiology |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
SecA
CROSS-LINKING ATPase RIBOSOME-BINDING Biophysics INSERTION SIGNAL-RECOGNITION PARTICLE Chromosomal translocation Arginine Biochemistry Bacterial Proteins Structural Biology Genetics membrane insertion Protein Precursors Molecular Biology Adenosine Triphosphatases Signal recognition particle ARCHITECTURE SecA Proteins protein translocation COLI MEMBRANE-VESICLES COMPLEX biology IDENTIFICATION Escherichia coli Proteins Cell Membrane Membrane Proteins Membrane Transport Proteins SecY Cell Biology Periplasmic space Transmembrane protein Protein Transport Transmembrane domain Secretory protein Amino Acid Substitution Membrane protein Mutation biology.protein bacteria STEPS PROTEIN-CONDUCTING CHANNEL SEC Translocation Channels |
| Zdroj: | FEBS Letters, 581(9), 1859-1864. Wiley |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2007.03.081 |
| Popis: | The Escherichia coli SecYEG complex forms a transmembrane channel for both protein export and membrane protein insertion. Secretory proteins and large periplasmic domains of membrane proteins require for translocation in addition the SecA ATPase. The conserved arginine 357 of SecY is essential for a yet unidentified step in the SecA catalytic cycle. To further dissect its role, we have analysed the requirement for 8357 in membrane protein insertion. Although 8357 substitutions abolish post-translational translocation, they allow the translocation of periplasmic domains targeted co-translationally by an N-terminal transmembrane segment. We propose that 8357 is essential for the initiation of SecA-dependent translocation only. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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