دورية أكاديمية
أعرض في EDS

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: Ranava D; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Yang Y; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Orenday-Tapia L; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Rousset F; Synthetic Biology Group, Microbiology Department, Institut Pasteur, Paris, France., Turlan C; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Morales V; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Cui L; Synthetic Biology Group, Microbiology Department, Institut Pasteur, Paris, France., Moulin C; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Froment C; Institut de Pharmacologie et de Biologie Structurale (IPBS), Université de Toulouse, CNRS, UPS, Toulouse, France., Munoz G; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Rech J; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Marcoux J; Institut de Pharmacologie et de Biologie Structurale (IPBS), Université de Toulouse, CNRS, UPS, Toulouse, France., Caumont-Sarcos A; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Albenne C; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France., Bikard D; Synthetic Biology Group, Microbiology Department, Institut Pasteur, Paris, France., Ieva R; Laboratoire de Microbiologie et Génétique Moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France.
المصدر: ELife [Elife] 2021 Apr 13; Vol. 10. Date of Electronic Publication: 2021 Apr 13.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: Bacterial Outer Membrane/*physiology , Bacterial Outer Membrane Proteins/*genetics , Escherichia coli/*genetics , Escherichia coli Proteins/*genetics , Lipoproteins/*genetics, Bacterial Outer Membrane Proteins/metabolism ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Genetic Fitness ; Lipoproteins/metabolism ; Protein Folding
مستخلص: 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 (σ E ) transcriptional response. σ E upregulates OMP biogenesis factors, including the β-barrel assembly machinery (BAM) that catalyses OMP folding. Here we report that DolP (formerly YraP), a σ E -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.
Competing Interests: DR, YY, LO, FR, CT, VM, LC, CM, CF, GM, JR, JM, AC, CA, DB, RI No competing interests declared
(© 2021, Ranava et al.)
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معلومات مُعتمدة: ATIP-Avenir Centre National de la Recherche Scientifique; ANR-10-INBS-08 Agence Nationale de la Recherche; ANR-10-LABX-62-IBEID Agence Nationale de la Recherche; PostDoc Fellowship Fondation pour la Recherche Médicale; 677823 International ERC_ European Research Council
فهرسة مساهمة: Keywords: BAM; DolP; E. coli; Envelope stress; OMPs; Outer membrane biogenesis; YraP; infectious disease; microbiology
المشرفين على المادة: 0 (Bacterial Outer Membrane Proteins)
0 (BamA protein, E coli)
0 (Escherichia coli Proteins)
0 (Lipoproteins)
تواريخ الأحداث: Date Created: 20210413 Date Completed: 20210913 Latest Revision: 20210913
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC8081527
DOI: 10.7554/eLife.67817
PMID: 33847565
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.67817