Dynamics of the localization of the plastid terminal oxidase inside the chloroplast

© The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 71(2020), 9 vom: 09. Mai, Seite 2661-2669
1. Verfasser: Bolte, Susanne (VerfasserIn)
Weitere Verfasser: Marcon, Elodie, Jaunario, Mélanie, Moyet, Lucas, Paternostre, Maité, Kuntz, Marcel, Krieger-Liszkay, Anja
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2020
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Alternative electron transport chloroplast confocal microscopy liposomes membrane association plastid terminal oxidase Oxidoreductases EC 1.-
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520 |a © The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com. 
520 |a The plastid terminal oxidase (PTOX) is a plastohydroquinone:oxygen oxidoreductase that shares structural similarities with alternative oxidases (AOXs). Multiple roles have been attributed to PTOX, such as involvement in carotene desaturation, a safety valve function, participation in the processes of chlororespiration, and setting the redox poise for cyclic electron transport. PTOX activity has been previously shown to depend on its localization at the thylakoid membrane. Here we investigate the dynamics of PTOX localization dependent on the proton motive force. Infiltrating illuminated leaves with uncouplers led to a partial dissociation of PTOX from the thylakoid membrane. In vitro reconstitution experiments showed that the attachment of purified recombinant maltose-binding protein (MBP)-OsPTOX to liposomes and isolated thylakoid membranes was strongest at slightly alkaline pH values in the presence of lower millimolar concentrations of KCl or MgCl2. In Arabidopsis thaliana overexpressing green fluorescent protein (GFP)-PTOX, confocal microscopy images showed that PTOX formed distinct spots in chloroplasts of dark-adapted or uncoupler-treated leaves, while the protein was more equally distributed in a network-like structure in the light. We propose a dynamic PTOX association with the thylakoid membrane depending on the presence of a proton motive force 
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650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Alternative electron transport 
650 4 |a chloroplast 
650 4 |a confocal microscopy 
650 4 |a liposomes 
650 4 |a membrane association 
650 4 |a plastid terminal oxidase 
650 7 |a Oxidoreductases  |2 NLM 
650 7 |a EC 1.-  |2 NLM 
700 1 |a Marcon, Elodie  |e verfasserin  |4 aut 
700 1 |a Jaunario, Mélanie  |e verfasserin  |4 aut 
700 1 |a Moyet, Lucas  |e verfasserin  |4 aut 
700 1 |a Paternostre, Maité  |e verfasserin  |4 aut 
700 1 |a Kuntz, Marcel  |e verfasserin  |4 aut 
700 1 |a Krieger-Liszkay, Anja  |e verfasserin  |4 aut 
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773 1 8 |g volume:71  |g year:2020  |g number:9  |g day:09  |g month:05  |g pages:2661-2669 
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