Gutenberg Open Science: The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-7124

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DC Field	Value	Language
dc.contributor.author	Tome-Stangl, Lydia	-
dc.contributor.author	Schätzel, Cornelia	-
dc.contributor.author	Tenzer, Stefan	-
dc.contributor.author	Bernhard, Frank	-
dc.contributor.author	Schneider, Dirk	-
dc.date.accessioned	2022-06-13T09:15:29Z	-
dc.date.available	2022-06-13T09:15:29Z	-
dc.date.issued	2017
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/7138	-
dc.description.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.	en_GB
dc.description.sponsorship	DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin	de
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.subject.ddc	500 Naturwissenschaften	de_DE
dc.subject.ddc	500 Natural sciences and mathematics	en_GB
dc.title	The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-7124	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 04 Medizin	de
jgu.organisation.department	FB 09 Chemie, Pharmazie u. Geowissensch.	de
jgu.organisation.number	2700	-
jgu.organisation.number	7950	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	PLOS ONE	de
jgu.journal.volume	12	de
jgu.journal.issue	12	de
jgu.pages.alternative	e0189532	de
jgu.publisher.year	2017	-
jgu.publisher.name	PLOS	de
jgu.publisher.place	San Francisco, California, US	de
jgu.publisher.uri	http://dx.doi.org/10.1371/journal.pone.0189532	de
jgu.publisher.issn	1932-6203	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	500	de
opus.date.modified	2018-04-26T09:59:10Z
opus.subject.dfgcode	00-000
opus.organisation.string	FB 09: Chemie, Pharmazie und Geowissenschaften: Institut für Pharmazie	de_DE
opus.organisation.string	FB 04: Medizin: Institut für Immunologie	de_DE
opus.identifier.opusid	58114
opus.institute.number	0908
opus.institute.number	0412
opus.metadataonly	false
opus.type.contenttype	Keine	de_DE
opus.type.contenttype	None	en_EN
opus.affiliated	Schätzel, Cornelia
opus.affiliated	Tenzer, Stefan
opus.affiliated	Schneider, Dirk
jgu.publisher.doi	10.1371/journal.pone.0189532	de
jgu.organisation.ror	https://ror.org/023b0x485
Appears in collections:	DFG-OA-Publizieren (2012 - 2017)

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