دورية أكاديمية
أعرض في EDS

Role of Ring6 in the Function of the E. coli MCE Protein LetB.

التفاصيل البيبلوغرافية
العنوان: Role of Ring6 in the Function of the E. coli MCE Protein LetB.
المؤلفون: Vieni C; Department of Cell Biology, New York University School of Medicine, New York, NY, USA; Department of Microbiology, New York University School of Medicine, New York, NY, USA., Coudray N; Department of Cell Biology, New York University School of Medicine, New York, NY, USA; Applied Bioinformatics Laboratories, New York University School of Medicine, New York, NY, USA., Isom GL; Department of Cell Biology, New York University School of Medicine, New York, NY, USA., Bhabha G; Department of Cell Biology, New York University School of Medicine, New York, NY, USA. Electronic address: gira.bhabha@gmail.com., Ekiert DC; Department of Cell Biology, New York University School of Medicine, New York, NY, USA; Department of Microbiology, New York University School of Medicine, New York, NY, USA. Electronic address: damian.ekiert@ekiertlab.org.
المصدر: Journal of molecular biology [J Mol Biol] 2022 Apr 15; Vol. 434 (7), pp. 167463. Date of Electronic Publication: 2022 Jan 22.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 2985088R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1089-8638 (Electronic) Linking ISSN: 00222836 NLM ISO Abbreviation: J Mol Biol Subsets: MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier
Original Publication: 1959- : London : Academic Press
مواضيع طبية MeSH: Escherichia coli*/genetics , Escherichia coli*/metabolism , Escherichia coli Proteins*/chemistry , Escherichia coli Proteins*/genetics , Membrane Proteins*/chemistry , Membrane Proteins*/genetics, Cell Membrane/metabolism ; Protein Domains
مستخلص: LetB is a tunnel-forming protein found in the cell envelope of some double-membraned bacteria, and is thought to be important for the transport of lipids between the inner and outer membranes. In Escherichia coli the LetB tunnel is formed from a stack of seven rings (Ring1 - Ring7), in which each ring is composed of a homo-hexameric assembly of MCE domains. The primary sequence of each MCE domain of the LetB protein is substantially divergent from the others, making each MCE ring unique in nature. The role of each MCE domain and how it contributes to the function of LetB is not well understood. Here we probed the importance of each MCE ring for the function of LetB, using a combination of bacterial growth assays and cryo-EM. Surprisingly, we find that ΔRing3 and ΔRing6 mutants, in which Ring3 and Ring6 have been deleted, confer increased resistance to membrane perturbing agents. Specific mutations in the pore-lining loops of Ring6 similarly confer increased resistance. A cryo-EM structure of the ΔRing6 mutant shows that despite the absence of Ring6, which leads to a shorter assembly, the overall architecture is maintained, highlighting the modular nature of MCE proteins. Previous work has shown that Ring6 is dynamic and in its closed state, may restrict the passage of substrate through the tunnel. Our work suggests that removal of Ring6 may relieve this restriction. The deletion of Ring6 combined with mutations in the pore-lining loops leads to a model for the tunnel gating mechanism of LetB. Together, these results provide insight into the functional roles of individual MCE domains and pore-lining loops in the LetB protein.
Competing Interests: Declaration of Interests The authors declare no competing interests.
(Copyright © 2022 Elsevier Ltd. All rights reserved.)
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معلومات مُعتمدة: F30 AI154907 United States AI NIAID NIH HHS; P30 CA016087 United States CA NCI NIH HHS; R00 GM112982 United States GM NIGMS NIH HHS; R35 GM128777 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: LetB; bacterial cell envelope; cryo-EM; lipid transport; microbiology
المشرفين على المادة: 0 (Escherichia coli Proteins)
0 (Membrane Proteins)
0 (YebT protein, E coli)
تواريخ الأحداث: Date Created: 20220125 Date Completed: 20220415 Latest Revision: 20230416
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC9112829
DOI: 10.1016/j.jmb.2022.167463
PMID: 35077766
قاعدة البيانات: MEDLINE
الوصف
تدمد:1089-8638
DOI:10.1016/j.jmb.2022.167463