The active protein-conducting channel of Escherichia coli contains an apolar patch
| Autor: | Redmar Bol, Janny G. de Wit, Arnold J. M. Driessen |
|---|---|
| Přispěvatelé: | Molecular Microbiology |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Vesicle-associated membrane protein 8
ENDOPLASMIC-RETICULUM CATALYTIC CYCLE Biology Models Biological Biochemistry Protein structure Escherichia coli Translocase ER MEMBRANE CHAPERONE SECB Cysteine TRANSLOCATION CHANNEL Molecular Biology Fluorescent Dyes Oxadiazoles Binding Sites Escherichia coli Proteins Endoplasmic reticulum PRECURSOR PROTEIN Membrane Proteins Water Cell Biology Translocon Protein Structure Tertiary Transport protein Protein Transport Spectrometry Fluorescence Secretory protein PLASMA-MEMBRANE Solvents Biophysics biology.protein CYTOPLASMIC MEMBRANE PREPROTEIN TRANSLOCASE DISULFIDE BRIDGE SEC Translocation Channels Bacterial Outer Membrane Proteins |
| Zdroj: | The Journal of Biological Chemistry, 282(41), 29785-29793. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| ISSN: | 0021-9258 |
| Popis: | Protein translocation across the cytoplasmic membrane of Escherichia coli is mediated by translocase, a complex of a protein conducting channel, SecYEG, and a peripheral motor domain, SecA. SecYEG has been proposed to constitute an aqueous path for proteins to pass the membrane in an unfolded state. To probe the solvation state of the active channel, the polarity sensitive fluorophore N-(( 2-( iodoacetoxy) ethyl)- N- methyl) amino- 7- nitrobenz- 2- oxa- 1,3- diazole was introduced at specific positions in the C- terminal region of the secretory protein proOmpA. Fluorescence measurements with defined proOmpA- DHFR translocation intermediates indicate mostly a water- exposed environment with a hydrophobic region in the center of the channel. |
| Databáze: | OpenAIRE |
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