Analysis of the chloroplast protein kinase Stt7 during state transitions.

State transitions allow for the balancing of the light excitation energy between photosystem I and photosystem II and for optimal photosynthetic activity when photosynthetic organisms are subjected to changing light conditions. This process is regulated by the redox state of the plastoquinone pool t...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Sylvain Lemeille, Adrian Willig, Nathalie Depège-Fargeix, Christian Delessert, Roberto Bassi, Jean-David Rochaix
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/0b26cc7fccef4fe98b19942a853ba7d5
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:0b26cc7fccef4fe98b19942a853ba7d5
record_format	dspace
spelling	oai:doaj.org-article:0b26cc7fccef4fe98b19942a853ba7d52021-11-25T05:33:47ZAnalysis of the chloroplast protein kinase Stt7 during state transitions.1544-91731545-788510.1371/journal.pbio.1000045https://doaj.org/article/0b26cc7fccef4fe98b19942a853ba7d52009-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19260761/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885State transitions allow for the balancing of the light excitation energy between photosystem I and photosystem II and for optimal photosynthetic activity when photosynthetic organisms are subjected to changing light conditions. This process is regulated by the redox state of the plastoquinone pool through the Stt7/STN7 protein kinase required for phosphorylation of the light-harvesting complex LHCII and for the reversible displacement of the mobile LHCII between the photosystems. We show that Stt7 is associated with photosynthetic complexes including LHCII, photosystem I, and the cytochrome b6f complex. Our data reveal that Stt7 acts in catalytic amounts. We also provide evidence that Stt7 contains a transmembrane region that separates its catalytic kinase domain on the stromal side from its N-terminal end in the thylakoid lumen with two conserved Cys that are critical for its activity and state transitions. On the basis of these data, we propose that the activity of Stt7 is regulated through its transmembrane domain and that a disulfide bond between the two lumen Cys is essential for its activity. The high-light-induced reduction of this bond may occur through a transthylakoid thiol-reducing pathway driven by the ferredoxin-thioredoxin system which is also required for cytochrome b6f assembly and heme biogenesis.Sylvain LemeilleAdrian WilligNathalie Depège-FargeixChristian DelessertRoberto BassiJean-David RochaixPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 7, Iss 3, p e45 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Sylvain Lemeille Adrian Willig Nathalie Depège-Fargeix Christian Delessert Roberto Bassi Jean-David Rochaix Analysis of the chloroplast protein kinase Stt7 during state transitions.
description	State transitions allow for the balancing of the light excitation energy between photosystem I and photosystem II and for optimal photosynthetic activity when photosynthetic organisms are subjected to changing light conditions. This process is regulated by the redox state of the plastoquinone pool through the Stt7/STN7 protein kinase required for phosphorylation of the light-harvesting complex LHCII and for the reversible displacement of the mobile LHCII between the photosystems. We show that Stt7 is associated with photosynthetic complexes including LHCII, photosystem I, and the cytochrome b6f complex. Our data reveal that Stt7 acts in catalytic amounts. We also provide evidence that Stt7 contains a transmembrane region that separates its catalytic kinase domain on the stromal side from its N-terminal end in the thylakoid lumen with two conserved Cys that are critical for its activity and state transitions. On the basis of these data, we propose that the activity of Stt7 is regulated through its transmembrane domain and that a disulfide bond between the two lumen Cys is essential for its activity. The high-light-induced reduction of this bond may occur through a transthylakoid thiol-reducing pathway driven by the ferredoxin-thioredoxin system which is also required for cytochrome b6f assembly and heme biogenesis.
format	article
author	Sylvain Lemeille Adrian Willig Nathalie Depège-Fargeix Christian Delessert Roberto Bassi Jean-David Rochaix
author_facet	Sylvain Lemeille Adrian Willig Nathalie Depège-Fargeix Christian Delessert Roberto Bassi Jean-David Rochaix
author_sort	Sylvain Lemeille
title	Analysis of the chloroplast protein kinase Stt7 during state transitions.
title_short	Analysis of the chloroplast protein kinase Stt7 during state transitions.
title_full	Analysis of the chloroplast protein kinase Stt7 during state transitions.
title_fullStr	Analysis of the chloroplast protein kinase Stt7 during state transitions.
title_full_unstemmed	Analysis of the chloroplast protein kinase Stt7 during state transitions.
title_sort	analysis of the chloroplast protein kinase stt7 during state transitions.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/0b26cc7fccef4fe98b19942a853ba7d5
work_keys_str_mv	AT sylvainlemeille analysisofthechloroplastproteinkinasestt7duringstatetransitions AT adrianwillig analysisofthechloroplastproteinkinasestt7duringstatetransitions AT nathaliedepegefargeix analysisofthechloroplastproteinkinasestt7duringstatetransitions AT christiandelessert analysisofthechloroplastproteinkinasestt7duringstatetransitions AT robertobassi analysisofthechloroplastproteinkinasestt7duringstatetransitions AT jeandavidrochaix analysisofthechloroplastproteinkinasestt7duringstatetransitions
_version_	1718414559410126848

Analysis of the chloroplast protein kinase Stt7 during state transitions.

Ejemplares similares