The Integration of YidC into the Cytoplasmic Membrane ofEscherichia coli Requires the Signal Recognition Particle, SecA and SecYEG
| Autor: | Karl Ludwig Schimz, Michael Moser, Matthias Müller, Hans-Georg Koch |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular chemistry [Bacterial Proteins] metabolism [Bacterial Proteins] metabolism [Signal Recognition Particle] Protein Conformation Biology Biochemistry metabolism [Cell Membrane] Cell membrane Bacterial Proteins ddc:570 secF protein Bacteria Escherichia coli medicine Inner membrane metabolism [Membrane Transport Proteins] SecF protein E coli Molecular Biology Adenosine Triphosphatases Signal recognition particle SecA Proteins Membrane transport protein isolation & purification [Bacterial Proteins] ultrastructure [Cell Membrane] Escherichia coli Proteins Cell Membrane Membrane Proteins Membrane Transport Proteins Cell Biology Periplasmic space SecA protein Bacteria Transmembrane domain medicine.anatomical_structure SecY protein E coli Membrane protein SecG protein E coli YIDC protein E coli Biophysics biology.protein metabolism [Escherichia coli] metabolism [Adenosine Triphosphatases] Signal Recognition Particle SEC Translocation Channels metabolism [Membrane Proteins] |
| Zdroj: | The journal of biological chemistry 277, 5715-5718 (2002). doi:10.1074/jbc.C100683200 |
| ISSN: | 0021-9258 |
| Popis: | The integration of the polytopic membrane protein YidC into the inner membrane of Escherichia coli was analyzed employing an in vitro system. Upon integration of in vitro synthesized YidC, a 42-kDa membrane protected fragment was detected, which could be immunoprecipitated with polyclonal anti-YidC antibodies. The occurrence of this fragment is in agreement with the predicted topology of YidC and probably encompasses the first two transmembrane domains and the connecting 320-amino acid-long periplasmic loop. The integration of YidC was strictly dependent on the signal recognition particle and SecA. YidC could not be integrated in the absence of SecY, SecE, or SecG, suggesting that YidC, in contrast to its mitochondrial orthologue Oxa1p, cannot engage a SecYEG-independent protein-conducting channel. |
| Databáze: | OpenAIRE |
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