دورية أكاديمية
أعرض في EDS

The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6.

التفاصيل البيبلوغرافية
العنوان: The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6.
المؤلفون: Tome-Stangl L; Institute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Mainz, Germany., Schaetzel C; Institute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Mainz, Germany., Tenzer S; Institute of Immunology, University Medical Center Mainz, Mainz, Germany., Bernhard F; Institute of Biophysical Chemistry, Goethe University Frankfurt am Main, Frankfurt am Main, Germany., Schneider D; Institute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Mainz, Germany.
المصدر: PloS one [PLoS One] 2017 Dec 14; Vol. 12 (12), pp. e0189532. Date of Electronic Publication: 2017 Dec 14 (Print Publication: 2017).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Cytochromes b6/*metabolism , Membrane Proteins/*metabolism, Amino Acid Sequence ; Cytochromes b6/chemistry ; Cytochromes b6/genetics ; Dimerization ; Membrane Proteins/chemistry ; Mutagenesis, Site-Directed ; Protein Folding ; Proteolysis ; Spinacia oleracea/enzymology
مستخلص: Studying folding and assembly of naturally occurring α-helical transmembrane proteins can inspire the design of membrane proteins with defined functions. Thus far, most studies have focused on the role of membrane-integrated protein regions. However, to fully understand folding pathways and stabilization of α-helical membrane proteins, it is vital to also include the role of soluble loops. We have analyzed the impact of interhelical loops on folding, assembly and stability of the heme-containing four-helix bundle transmembrane protein cytochrome b6 that is involved in charge transfer across biomembranes. Cytochrome b6 consists of two transmembrane helical hairpins that sandwich two heme molecules. Our analyses strongly suggest that the loop connecting the helical hairpins is not crucial for positioning the two protein "halves" for proper folding and assembly of the holo-protein. Furthermore, proteolytic removal of any of the remaining two loops, which connect the two transmembrane helices of a hairpin structure, appears to also not crucially effect folding and assembly. Overall, the transmembrane four-helix bundle appears to be mainly stabilized via interhelical interactions in the transmembrane regions, while the soluble loop regions guide assembly and stabilize the holo-protein. The results of this study might steer future strategies aiming at designing heme-binding four-helix bundle structures, involved in transmembrane charge transfer reactions.
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المشرفين على المادة: 0 (Cytochromes b6)
0 (Membrane Proteins)
تواريخ الأحداث: Date Created: 20171215 Date Completed: 20171229 Latest Revision: 20181113
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC5730185
DOI: 10.1371/journal.pone.0189532
PMID: 29240839
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0189532