Protein complex within Escherichia coli inner membrane. TolA N-terminal domain interacts with TolQ and TolR proteins
| Autor: | Derouiche, R, Bénédetti, H, Lazzaroni, JC, Lazdunski, C, Lloubès, R |
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| Přispěvatelé: | Laboratoire d'ingénierie des systèmes macromoléculaires (LISM), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU) |
| Rok vydání: | 1995 |
| Předmět: |
Base Sequence
Genotype [SDV]Life Sciences [q-bio] Escherichia coli Proteins Cell Membrane Immunoblotting Molecular Sequence Data Restriction Mapping Membrane Proteins Recombinant Proteins Models Structural Molecular Weight Cross-Linking Reagents Bacterial Proteins Oligodeoxyribonucleotides Formaldehyde Escherichia coli Cloning Molecular Plasmids |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, 1995, 270 (19), pp.11078-11084. ⟨10.1074/jbc.270.19.11078⟩ Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1995, 270 (19), pp.11078-11084. ⟨10.1074/jbc.270.19.11078⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.270.19.11078⟩ |
| Popis: | International audience; The TolA, TolB, TolQ, and TolR proteins are involved in maintaining the integrity of the Escherichia coli outer membrane and in the import of group A colicins and filamentous phage DNA. TolA, TolQ, and TolR are localized in the inner membrane while TolB is periplasmic, although a small amount of membrane-associated TolB is always found. In vivo cross-linking experiments with formaldehyde were performed in order to determine the proteins interacting with TolA. In wild-type strains, two specific complexes of 65 and 71 kDa, comprising TolA, were identified. These complexes were absent in a tolQ strain, while only the 65-kDa complex was absent in a tolR strain. When the tol strains were transformed with plasmids encoding TolR or TolQ, the specific complexes were restored. Moreover, immunoprecipitation experiments with the antiserum directed against TolA indicated that TolQ and TolR were co-immunoprecipitated with TolA after cross-linking. These data demonstrate that TolA interacts directly with TolR and TolQ. Two truncated TolA proteins devoid of either the C-terminal or the central domains of the protein were subjected to in vivo cross-linking. Since these two TolA derivatives still formed specific complexes with TolR derivatives still formed specific complexes with TolR and TolQ, we concluded that the TolA N-terminal domain interacted with these proteins. |
| Databáze: | OpenAIRE |
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