Lipoprotein DolP supports proper folding of BamA in the bacterial outer membrane promoting fitness upon envelope stress

التفاصيل البيبلوغرافية
العنوان: Lipoprotein DolP supports proper folding of BamA in the bacterial outer membrane promoting fitness upon envelope stress
المؤلفون: Cyril Moulin, Yiying Yang, Violette Morales, Jérôme Rech, Gladys Munoz, Cécile Albenne, David Ranava, Raffaele Ieva, David Bikard, Lun Cui, Julien Marcoux, Anne Caumont-Sarcos, Catherine Turlan, François Rousset, Luis Orenday-Tapia, Carine Froment
المساهمون: Laboratoire de microbiologie et génétique moléculaires - UMR5100 (LMGM), Centre de Biologie Intégrative (CBI), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Biologie de Synthèse - Synthetic biology, Institut Pasteur [Paris] (IP), Institut de pharmacologie et de biologie structurale (IPBS), Further financial support was provided by: the Fondation pour la Recherche Médicale to DR, the Chinese Scholarship Council as part of a joint international PhD program with Toulouse University Paul Sabatier to YY, the French Ministry of Higher Education and Research to LO-T, the Ecole Normale Supérieure to FR, the European Research Council (Europe Union’s Horizon 2020 research and innovation program, grant agreement No 677823), the French governmental Investissement d'Avenir program and the Laboratoire d’Excellence ‘Integrative Biology of Emerging Infectious Diseases’ (ANR-10-LABX-62-IBEID) to DB, the Centre National de la Recherche Scientifique and the ATIP-Avenir program to RI., ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), European Project: 677823,H2020,ERC-2015-STG,CRISPAIR(2016), Laboratoire de microbiologie et génétique moléculaires (LMGM), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris], Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées
المصدر: eLife, Vol 10 (2021)
eLife
eLife, 2021, 10, pp.e67817. ⟨10.7554/eLife.67817⟩
eLife, eLife Sciences Publication, 2021, 10, pp.e67817. ⟨10.7554/eLife.67817⟩
بيانات النشر: eLife Sciences Publications Ltd, 2021.
سنة النشر: 2021
مصطلحات موضوعية: Protein Folding, Cell division, QH301-705.5, Lipoproteins, Science, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Bama, Escherichia coli, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Biology (General), 030304 developmental biology, Envelope (waves), 0303 health sciences, Microbiology and Infectious Disease, BAM, General Immunology and Microbiology, Chemistry, Outer membrane biogenesis, General Neuroscience, Escherichia coli Proteins, E. coli, Envelope stress, General Medicine, DolP, bacterial infections and mycoses, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, YraP, Cell biology, Folding (chemistry), Bacterial Outer Membrane, bacteria, Medicine, Peptidoglycan, Genetic Fitness, Bacterial outer membrane, OMPs, 030217 neurology & neurosurgery, Biogenesis, Lipoprotein, Research Article, Bacterial Outer Membrane Proteins
الوصف: In Proteobacteria, integral outer membrane proteins (OMPs) are crucial for the maintenance of the envelope permeability barrier to some antibiotics and detergents. In Enterobacteria, envelope stress caused by unfolded OMPs activates the sigmaE (σE) transcriptional response. σE upregulates OMP biogenesis factors, including the β-barrel assembly machinery (BAM) that catalyses OMP folding. Here we report that DolP (formerly YraP), a σE-upregulated and poorly understood outer membrane lipoprotein, is crucial for fitness in cells that undergo envelope stress. We demonstrate that DolP interacts with the BAM complex by associating with outer membrane-assembled BamA. We provide evidence that DolP is important for proper folding of BamA that overaccumulates in the outer membrane, thus supporting OMP biogenesis and envelope integrity. Notably, mid-cell recruitment of DolP had been linked to regulation of septal peptidoglycan remodelling by an unknown mechanism. We now reveal that, during envelope stress, DolP loses its association with the mid-cell, thereby suggesting a mechanistic link between envelope stress caused by impaired OMP biogenesis and the regulation of a late step of cell division.
اللغة: English
تدمد: 2050-084X
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::930ae36ec490dff2b62bd1379a210f42
https://elifesciences.org/articles/67817
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....930ae36ec490dff2b62bd1379a210f42
قاعدة البيانات: OpenAIRE