The lipopolysaccharide-transporter complex LptB2FG also displays adenylate kinase activity in vitro dependent on the binding partners LptC/LptA
| العنوان: | The lipopolysaccharide-transporter complex LptB2FG also displays adenylate kinase activity in vitro dependent on the binding partners LptC/LptA |
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| المؤلفون: | Cédric Laguri, Isabel Ayala, Karine Giandoreggio-Barranco, Jean-Pierre Simorre, Tiago Baeta, Paola Sperandeo, Elisabete C.C. M. Moura, Alessandra Polissi |
| المساهمون: | Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA) |
| المصدر: | The Journal of Biological Chemistry Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2021, pp.101313. ⟨10.1016/j.jbc.2021.101313⟩ Journal of Biological Chemistry, 2021, pp.101313. ⟨10.1016/j.jbc.2021.101313⟩ |
| بيانات النشر: | American Society for Biochemistry and Molecular Biology, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | Lipopolysaccharides, Models, Molecular, Accelerated Communication, nuclear magnetic resonance (NMR), ATPase, STD, saturation transfer difference, Adenylate kinase, ATP-binding cassette transporter, Biochemistry, adenylate kinase, Lipopolysaccharide transport, 03 medical and health sciences, 0302 clinical medicine, Adenosine Triphosphate, Escherichia coli, Inner membrane, AK, adenylate kinase, Molecular Biology, OM, outer membrane, 030304 developmental biology, 0303 health sciences, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, Chemistry, Escherichia coli Proteins, Membrane Proteins, Biological Transport, Cell Biology, Periplasmic space, LptAm, monomeric version of LptA, Transmembrane protein, NMR, Cell biology, IM, inner membrane, TBS, Tris-buffered saline, biology.protein, SMA, styrene-maleic acid, cell wall, LPS, lipopolysaccharide, ATP-Binding Cassette Transporters, ABC transporter, Bacterial outer membrane, Carrier Proteins, 030217 neurology & neurosurgery, lipopolysaccharide (LPS), Lpt, lipopolysaccharide transporter system, TM, transmembrane |
| الوصف: | Lipopolysaccharide (LPS) is an essential glycolipid that covers the surface of gram-negative bacteria. The transport of LPS involves a dedicated seven-protein transporter system called the lipopolysaccharide transport system (Lpt) machinery that physically spans the entire cell envelope. The LptB2FG complex is an ABC transporter that hydrolyzes ATP to extract LPS from the inner membrane for transport to the outer membrane. Here, we extracted LptB2FG directly from the inner membrane with its original lipid environment using styrene-maleic acid polymers. We found that styrene-maleic acid polymers-LptB2FG in nanodiscs display not only ATPase activity but also a previously uncharacterized adenylate kinase (AK) activity, as it catalyzed phosphotransfer between two ADP molecules to generate ATP and AMP. The ATPase and AK activities of LptB2FG were both stimulated by the interaction on the periplasmic side with the periplasmic LPS transport proteins LptC and LptA and inhibited by the presence of the LptC transmembrane helix. We determined that the isolated ATPase module (LptB) had weak AK activity in the absence of transmembrane proteins LptF and LptG, and one mutation in LptB that weakens its affinity for ADP led to AK activity similar to that of fully assembled complex. Thus, we conclude that LptB2FG is capable of producing ATP from ADP, depending on the assembly of the Lpt bridge, and that this AK activity might be important to ensure efficient LPS transport in the fully assembled Lpt system. |
| اللغة: | English |
| تدمد: | 1083-351X 0021-9258 |
| DOI: | 10.1016/j.jbc.2021.101313⟩ |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::018f1cad516d0bb6de3e883a7812f6f8 http://europepmc.org/articles/PMC8633020 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....018f1cad516d0bb6de3e883a7812f6f8 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 1083351X 00219258 |
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| DOI: | 10.1016/j.jbc.2021.101313⟩ |