دورية أكاديمية
أعرض في EDS

A general protocol for the expression and purification of the intact transmembrane transporter FeoB.

التفاصيل البيبلوغرافية
العنوان: A general protocol for the expression and purification of the intact transmembrane transporter FeoB.
المؤلفون: Sestok AE; Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD, 21250, USA., O'Sullivan SM; Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD, 21250, USA., Smith AT; Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD, 21250, USA. Electronic address: smitha@umbc.edu.
المصدر: Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2022 Sep 01; Vol. 1864 (9), pp. 183973. Date of Electronic Publication: 2022 May 27.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101731713 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-2642 (Electronic) Linking ISSN: 00052736 NLM ISO Abbreviation: Biochim Biophys Acta Biomembr Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Amsterdam : Elsevier
مواضيع طبية MeSH: Cation Transport Proteins*/metabolism , Escherichia coli Proteins*/genetics , Escherichia coli Proteins*/metabolism, Biological Transport ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Iron/metabolism ; Membrane Transport Proteins/metabolism ; Virulence
مستخلص: Ferrous iron (Fe 2+ ) transport is an essential process that supports the growth, intracellular survival, and virulence of several drug-resistant pathogens, and the ferrous iron transport (Feo) system is the most important and widespread protein complex that mediates Fe 2+ transport in these organisms. The Feo system canonically comprises three proteins (FeoA/B/C). FeoA and FeoC are both small, accessory proteins localized to the cytoplasm, and their roles in the Fe 2+ transport process have been of great debate. FeoB is the only wholly-conserved component of the Feo system and serves as the inner membrane-embedded Fe 2+ transporter with a soluble G-protein-like N-terminal domain. In vivo studies have underscored the importance of Feo during infection, emphasizing the need to better understand Feo-mediated Fe 2+ uptake, although a paucity of research exists on intact FeoB. To surmount this problem, we designed an overproduction and purification system that can be applied generally to a suite of intact FeoBs from several organisms. Importantly, we noted that FeoB is extremely sensitive to excess salt while in the membrane of a recombinant host, and we designed a workflow to circumvent this issue. We also demonstrated effective protein extraction from the lipid bilayer through small-scale solubilization studies. We then applied this approach to the large-scale purifications of Escherichia coli and Pseudomonas aeruginosa FeoBs to high purity and homogeneity. Lastly, we show that our protocol can be generally applied to various FeoB proteins. Thus, this workflow allows for isolation of suitable quantities of FeoB for future biochemical and biophysical characterization.
(Copyright © 2022 Elsevier B.V. All rights reserved.)
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معلومات مُعتمدة: R21 DE027803 United States DE NIDCR NIH HHS; R35 GM133497 United States GM NIGMS NIH HHS; T32 GM066706 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: Feo system; GTPase; Iron; Iron transport; Membrane transporter
المشرفين على المادة: 0 (Cation Transport Proteins)
0 (Escherichia coli Proteins)
0 (FeoB protein, E coli)
0 (Membrane Transport Proteins)
E1UOL152H7 (Iron)
تواريخ الأحداث: Date Created: 20220531 Date Completed: 20220617 Latest Revision: 20220902
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC9203943
DOI: 10.1016/j.bbamem.2022.183973
PMID: 35636558
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-2642
DOI:10.1016/j.bbamem.2022.183973