Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-6735
Authors: Junglas, Benedikt
Siebenaller, Carmen
Schlösser, Lukas
Hellmann, Nadja
Schneider, Dirk
Title: GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity
Online publication date: 28-Jan-2022
Language: english
Abstract: The function of IM30 (also known as Vipp1) is linked to protection and/or remodeling of the thylakoid membrane system in chloroplasts and cyanobacteria. Recently, it has been revealed that the Arabidopsis IM30 protein exhibits GTP hydrolyzing activity in vitro, which was unexpected, as IM30 does not show any classical GTPase features. In the present study, we addressed the question, whether an apparent GTPase activity is conserved in IM30 proteins and can also be observed for IM30 of the cyanobacterium Synechocystis sp. PCC 6803. We show that Synechocystis IM30 is indeed able to bind and hydrolyze GTP followed by the release of Pi. Yet, the apparent GTPase activity of Synechocystis IM30 does not depend on Mg2+, which, together with the lack of classical GTPase features, renders IM30 an atypical GTPase. To elucidate the impact of this cryptic GTPase activity on the membrane remodeling activity of IM30, we tested whether GTP hydrolysis influences IM30 membrane binding and/or IM30-mediated membrane fusion. We show that membrane remodeling by Synechocystis IM30 is slightly affected by nucleotides. Yet, despite IM30 clearly catalyzing GTP hydrolysis, this does not seem to be vital for its membrane remodeling function.
DDC: 540 Chemie
540 Chemistry and allied sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 09 Chemie, Pharmazie u. Geowissensch.
Place: Mainz
ROR: https://ror.org/023b0x485
DOI: http://doi.org/10.25358/openscience-6735
Version: Published version
Publication type: Zeitschriftenaufsatz
License: CC BY
Information on rights of use: https://creativecommons.org/licenses/by/4.0/
Journal: Scientific reports
10
Pages or article number: 9793
Publisher: Macmillan Publishers Limited, part of Springer Nature
Publisher place: London
Issue date: 2020
ISSN: 2045-2322
Publisher URL: https://doi.org/10.1038/s41598-020-66818-9
Publisher DOI: 10.1038/s41598-020-66818-9
Appears in collections:JGU-Publikationen

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