The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Lydia Tome-Stangl
- Cornelia Schätzel
- Stefan Tenzer
- Frank Bernhard
- Dirk Schneider
- Sammlungen
- metadata
- ISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 12
- Zeitschrift
- PLOS ONE
- Schlüsselwörter
- 500 Naturwissenschaften
- 500 Natural sciences and mathematics
- Sprache
- eng
- Paginierung
- e0189532
- Datum der Veröffentlichung
- 2017
- Herausgeber
- PLOS
- Herausgeber URL
- http://dx.doi.org/10.1371/journal.pone.0189532
- Datum der Datenerfassung
- 2020
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2020
- Zugang
- Public
- Titel
- The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6
- Ausgabe der Zeitschrift
- 12
Datenquelle: METADATA.UB
- Andere Metadatenquellen:
-
- Autoren
- Lydia Tome-Stangl
- Cornelia Schaetzel
- Stefan Tenzer
- Frank Bernhard
- Dirk Schneider
- DOI
- 10.1371/journal.pone.0189532
- Editoren
- Eric Cascales
- eISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 12
- Zeitschrift
- PLOS ONE
- Sprache
- en
- Online publication date
- 2017
- Paginierung
- e0189532 - e0189532
- Status
- Published online
- Herausgeber
- Public Library of Science (PLoS)
- Herausgeber URL
- http://dx.doi.org/10.1371/journal.pone.0189532
- Datum der Datenerfassung
- 2022
- Titel
- The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6
- Ausgabe der Zeitschrift
- 12
Datenquelle: Crossref
- Abstract
- 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.
- Addresses
- Institute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Mainz, Germany.
- Autoren
- Lydia Tome-Stangl
- Cornelia Schaetzel
- Stefan Tenzer
- Frank Bernhard
- Dirk Schneider
- DOI
- 10.1371/journal.pone.0189532
- eISSN
- 1932-6203
- Externe Identifier
- PubMed Identifier: 29240839
- PubMed Central ID: PMC5730185
- Open access
- true
- ISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 12
- Zeitschrift
- PloS one
- Schlüsselwörter
- Spinacia oleracea
- Cytochromes b6
- Membrane Proteins
- Mutagenesis, Site-Directed
- Amino Acid Sequence
- Protein Folding
- Dimerization
- Proteolysis
- Sprache
- eng
- Medium
- Electronic-eCollection
- Online publication date
- 2017
- Open access status
- Open Access
- Paginierung
- e0189532
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2017
- Titel
- The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6.
- Sub types
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 12
Files
https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0189532&type=printable https://europepmc.org/articles/PMC5730185?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- 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.
- Date of acceptance
- 2017
- Autoren
- Lydia Tome-Stangl
- Cornelia Schaetzel
- Stefan Tenzer
- Frank Bernhard
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/29240839
- DOI
- 10.1371/journal.pone.0189532
- eISSN
- 1932-6203
- Externe Identifier
- PubMed Central ID: PMC5730185
- Ausgabe der Veröffentlichung
- 12
- Zeitschrift
- PLoS One
- Schlüsselwörter
- Amino Acid Sequence
- Cytochromes b6
- Dimerization
- Membrane Proteins
- Mutagenesis, Site-Directed
- Protein Folding
- Proteolysis
- Spinacia oleracea
- Sprache
- eng
- Country
- United States
- Paginierung
- e0189532
- PII
- PONE-D-17-25489
- Datum der Veröffentlichung
- 2017
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2017
- Titel
- The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 12
Datenquelle: PubMed
- Author's licence
- CC-BY
- Autoren
- Lydia Tome-Stangl
- Cornelia Schätzel
- Stefan Tenzer
- Frank Bernhard
- Dirk Schneider
- Hosting institution
- Universitätsbibliothek Mainz
- Sammlungen
- DFG-OA-Publizieren (2012 - 2017)
- Resource version
- Published version
- DOI
- 10.1371/journal.pone.0189532
- Funding acknowledgements
- DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin
- File(s) embargoed
- false
- Open access
- true
- ISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 12
- Zeitschrift
- PLOS ONE
- Schlüsselwörter
- 500 Naturwissenschaften
- 500 Natural sciences and mathematics
- Sprache
- eng
- Open access status
- Open Access
- Paginierung
- e0189532
- Datum der Veröffentlichung
- 2017
- Public URL
- https://openscience.ub.uni-mainz.de/handle/20.500.12030/7138
- Herausgeber
- PLOS
- Herausgeber URL
- http://dx.doi.org/10.1371/journal.pone.0189532
- Datum der Datenerfassung
- 2022
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2022
- Zugang
- Public
- Titel
- The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6
- Ausgabe der Zeitschrift
- 12
Files
the_soluble_loop_bc_region_gu-20220612152254088.pdf
Datenquelle: OPENSCIENCE.UB
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