Gutenberg Open Science: Binding and/or hydrolysis of purine-based nucleotides is not required for IM30 ring formation

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-8072

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DC Field	Value	Language
dc.contributor.author	Siebenaller, Carmen	-
dc.contributor.author	Schlösser, Lukas	-
dc.contributor.author	Junglas, Benedikt	-
dc.contributor.author	Schmidt-Dengler, Martina	-
dc.contributor.author	Jacob, Dominik	-
dc.contributor.author	Hellmann, Nadja	-
dc.contributor.author	Sachse, Carsten	-
dc.contributor.author	Helm, Mark	-
dc.contributor.author	Schneider, Dirk	-
dc.date.accessioned	2022-11-11T08:37:20Z	-
dc.date.available	2022-11-11T08:37:20Z	-
dc.date.issued	2021	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/8087	-
dc.description.abstract	IM30, the inner membrane-associated protein of 30 kDa, is conserved in cyanobacteria and chloroplasts. Although its exact physiological function is still mysterious, IM30 is clearly essential for thylakoid membrane biogenesis and/or dynamics. Recently, a cryptic IM30 GTPase activity has been reported, albeit thus far no physiological function has been attributed to this. Yet, it is still possible that GTP binding/hydrolysis affects formation of the prototypical large homo-oligomeric IM30 ring and rod structures. Here, we show that the Synechocystis sp. PCC 6803 IM30 protein in fact is an NTPase that hydrolyzes GTP and ATP, but not CTP or UTP, with about identical rates. While IM30 forms large oligomeric ring complexes, nucleotide binding and/or hydrolysis are clearly not required for ring formation.	en_GB
dc.language.iso	eng	de
dc.rights	CC BY-NC-ND	*
dc.rights.uri	https://creativecommons.org/licenses/by-nc-nd/4.0/	*
dc.subject.ddc	540 Chemie	de_DE
dc.subject.ddc	540 Chemistry and allied sciences	en_GB
dc.subject.ddc	570 Biowissenschaften	de_DE
dc.subject.ddc	570 Life sciences	en_GB
dc.title	Binding and/or hydrolysis of purine-based nucleotides is not required for IM30 ring formation	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-8072	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 09 Chemie, Pharmazie u. Geowissensch.	de
jgu.organisation.number	7950	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	FEBS letters	de
jgu.journal.volume	595	de
jgu.journal.issue	14	de
jgu.pages.start	1876	de
jgu.pages.end	1885	de
jgu.publisher.year	2021	-
jgu.publisher.name	Wiley	de
jgu.publisher.place	Chichester	de
jgu.publisher.issn	1873-3468	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	540	de
jgu.subject.ddccode	570	de
jgu.publisher.doi	10.1002/1873-3468.14140	de
jgu.organisation.ror	https://ror.org/023b0x485	-
Appears in collections:	JGU-Publikationen

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