Small membranous proteins of the TorE/NapE family, crutches for cognate respiratory systems in Proteobacteria
- In this report, we investigate small proteins involved in bacterial alternative respiratory systems that improve the enzymatic efficiency through better anchorage and multimerization of membrane components. Using the small protein TorE of the respiratory TMAO reductase system as a model, we discovered that TorE is part of a subfamily of small proteins that are present in proteobacteria in which they play a similar role for bacterial respiratory systems. We reveal by microscopy that, in Shewanella oneidensis MR1, alternative respiratory systems are evenly distributed in the membrane contrary to what has been described for Escherichia coli. Thus, the better efficiency of the respiratory systems observed in the presence of the small proteins is not due to a specific localization in the membrane, but rather to the formation of membranous complexes formed by TorE homologs with their c-type cytochrome partner protein. By an in vivo approach combining Clear Native electrophoresis and fluorescent translational fusions, we determined the 4: 4In this report, we investigate small proteins involved in bacterial alternative respiratory systems that improve the enzymatic efficiency through better anchorage and multimerization of membrane components. Using the small protein TorE of the respiratory TMAO reductase system as a model, we discovered that TorE is part of a subfamily of small proteins that are present in proteobacteria in which they play a similar role for bacterial respiratory systems. We reveal by microscopy that, in Shewanella oneidensis MR1, alternative respiratory systems are evenly distributed in the membrane contrary to what has been described for Escherichia coli. Thus, the better efficiency of the respiratory systems observed in the presence of the small proteins is not due to a specific localization in the membrane, but rather to the formation of membranous complexes formed by TorE homologs with their c-type cytochrome partner protein. By an in vivo approach combining Clear Native electrophoresis and fluorescent translational fusions, we determined the 4: 4 stoichiometry of the complexes. In addition, mild solubilization of the cytochrome indicates that the presence of the small protein reinforces its anchoring to the membrane. Therefore, assembly of the complex induced by this small protein improves the efficiency of the respiratory system.…
Author details: | Olivier N. LemaireORCiD, Pascale InfossiORCiD, Amine Ali Chaouche, Leon Espinosa, Silke LeimkühlerORCiDGND, Marie-Thérèse Giudici-Orticoni, Vincent MéjeanORCiD, Chantal Iobbi-Nivol |
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URN: | urn:nbn:de:kobv:517-opus4-459208 |
DOI: | https://doi.org/10.25932/publishup-45920 |
ISSN: | 1866-8372 |
Title of parent work (German): | Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe |
Publication series (Volume number): | Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe (933) |
Publication type: | Postprint |
Language: | English |
Date of first publication: | 2020/06/03 |
Publication year: | 2018 |
Publishing institution: | Universität Potsdam |
Release date: | 2020/06/03 |
Tag: | c-type cytochromes; cytochrome bd oxidase; escherichia-coli; microbiology; microbiology techniques; molybdenum cofactor biosynthesis; mutational analysis; native electrophoresis; nitrate; reductase; swiss-model; trimethylamine n-oxide |
Issue: | 933 |
Number of pages: | 15 |
Source: | Scientific Reports 8 (2018) 13576 DOI: 10.1038/s41598-018-31851-2 |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät |
DDC classification: | 5 Naturwissenschaften und Mathematik / 50 Naturwissenschaften / 500 Naturwissenschaften und Mathematik |
6 Technik, Medizin, angewandte Wissenschaften / 60 Technik / 600 Technik, Technologie | |
Peer review: | Referiert |
Publishing method: | Open Access |
License (German): | CC-BY - Namensnennung 4.0 International |
External remark: | Bibliographieeintrag der Originalveröffentlichung/Quelle |