GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Abstract
- <jats:title>Abstract</jats:title><jats:p>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 <jats:italic>Arabidopsis</jats:italic> IM30 protein exhibits GTP hydrolyzing activity <jats:italic>in vitro</jats:italic>, 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 <jats:italic>Synechocystis</jats:italic> sp. PCC 6803. We show that <jats:italic>Synechocystis</jats:italic> IM30 is indeed able to bind and hydrolyze GTP followed by the release of P<jats:sub>i</jats:sub>. Yet, the apparent GTPase activity of <jats:italic>Synechocystis</jats:italic> IM30 does not depend on Mg<jats:sup>2+</jats:sup>, 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 <jats:italic>Synechocystis</jats:italic> 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.</jats:p>
- Autoren
- Benedikt Junglas
- Carmen Siebenaller
- Lukas Schlösser
- Nadja Hellmann
- Dirk Schneider
- DOI
- 10.1038/s41598-020-66818-9
- eISSN
- 2045-2322
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- Scientific Reports
- Sprache
- en
- Artikelnummer
- 9793
- Online publication date
- 2020
- Status
- Published online
- Herausgeber
- Springer Science and Business Media LLC
- Herausgeber URL
- http://dx.doi.org/10.1038/s41598-020-66818-9
- Datum der Datenerfassung
- 2022
- Titel
- GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity
- Ausgabe der Zeitschrift
- 10
Datenquelle: Crossref
- Andere Metadatenquellen:
-
- 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 P<sub>i</sub>. Yet, the apparent GTPase activity of Synechocystis IM30 does not depend on Mg<sup>2+</sup>, 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.
- Addresses
- Department of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, 55128, Mainz, Germany.
- Autoren
- Benedikt Junglas
- Carmen Siebenaller
- Lukas Schlösser
- Nadja Hellmann
- Dirk Schneider
- DOI
- 10.1038/s41598-020-66818-9
- eISSN
- 2045-2322
- Externe Identifier
- PubMed Identifier: 32555292
- PubMed Central ID: PMC7299955
- Open access
- true
- ISSN
- 2045-2322
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- Scientific reports
- Schlüsselwörter
- Cell Membrane
- Synechocystis
- Magnesium
- GTP Phosphohydrolases
- Nucleotides
- Bacterial Proteins
- Membrane Proteins
- Guanosine Triphosphate
- Membrane Fusion
- Protein Binding
- Hydrolysis
- Sprache
- eng
- Medium
- Electronic
- Online publication date
- 2020
- Open access status
- Open Access
- Paginierung
- 9793
- Datum der Veröffentlichung
- 2020
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2020
- Titel
- GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 10
Files
https://www.nature.com/articles/s41598-020-66818-9.pdf https://europepmc.org/articles/PMC7299955?pdf=render
Datenquelle: Europe PubMed Central
- 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.
- Date of acceptance
- 2020
- Autoren
- Benedikt Junglas
- Carmen Siebenaller
- Lukas Schlösser
- Nadja Hellmann
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/32555292
- DOI
- 10.1038/s41598-020-66818-9
- eISSN
- 2045-2322
- Externe Identifier
- PubMed Central ID: PMC7299955
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- Sci Rep
- Schlüsselwörter
- Bacterial Proteins
- Cell Membrane
- GTP Phosphohydrolases
- Guanosine Triphosphate
- Hydrolysis
- Magnesium
- Membrane Fusion
- Membrane Proteins
- Nucleotides
- Protein Binding
- Synechocystis
- Sprache
- eng
- Country
- England
- Paginierung
- 9793
- PII
- 10.1038/s41598-020-66818-9
- Datum der Veröffentlichung
- 2020
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2020
- Titel
- GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 10
Datenquelle: PubMed
- Author's licence
- CC-BY
- Autoren
- Benedikt Junglas
- Carmen Siebenaller
- Lukas Schlösser
- Nadja Hellmann
- Dirk Schneider
- Hosting institution
- Universitätsbibliothek Mainz
- Sammlungen
- JGU-Publikationen
- Resource version
- Published version
- DOI
- 10.1038/s41598-020-66818-9
- Funding acknowledgements
- Open Access-Publizieren Universität Mainz / Universitätsmedizin Mainz
- File(s) embargoed
- false
- Open access
- true
- ISSN
- 2045-2322
- Zeitschrift
- Scientific reports
- Schlüsselwörter
- 540 Chemie
- 540 Chemistry and allied sciences
- Sprache
- eng
- Open access status
- Open Access
- Paginierung
- 9793
- Datum der Veröffentlichung
- 2020
- Public URL
- https://openscience.ub.uni-mainz.de/handle/20.500.12030/6746
- Herausgeber
- Macmillan Publishers Limited, part of Springer Nature
- Herausgeber URL
- https://doi.org/10.1038/s41598-020-66818-9
- Datum der Datenerfassung
- 2022
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2022
- Zugang
- Public
- Titel
- GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity
- Ausgabe der Zeitschrift
- 10
Files
gtp_hydrolysis_by_synechocyst-20220128101832259.pdf
Datenquelle: OPENSCIENCE.UB
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