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The key cyclic electron flow protein PGR5 associates with cytochrome b(6)f, and its function is partially influenced by the LHCII state transition

In plants and algae, PGR5-dependent cyclic electron flow (CEF) is an important regulator of acclimation to fluctuating environments, but how PGR5 participates in CEF is unclear. In this work, we analyzed two PGR5s in cucumber (Cucumis sativus L.) under different conditions and found that CsPGR5a pla...

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Autores principales: Wu, Xinyi, Wu, Jianqiang, Wang, Yu, He, Meiwen, He, Mingming, Liu, Weikang, Shu, Sheng, Sun, Jin, Guo, Shirong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7933433/
https://www.ncbi.nlm.nih.gov/pubmed/33664242
http://dx.doi.org/10.1038/s41438-021-00460-y
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author Wu, Xinyi
Wu, Jianqiang
Wang, Yu
He, Meiwen
He, Mingming
Liu, Weikang
Shu, Sheng
Sun, Jin
Guo, Shirong
author_facet Wu, Xinyi
Wu, Jianqiang
Wang, Yu
He, Meiwen
He, Mingming
Liu, Weikang
Shu, Sheng
Sun, Jin
Guo, Shirong
author_sort Wu, Xinyi
collection PubMed
description In plants and algae, PGR5-dependent cyclic electron flow (CEF) is an important regulator of acclimation to fluctuating environments, but how PGR5 participates in CEF is unclear. In this work, we analyzed two PGR5s in cucumber (Cucumis sativus L.) under different conditions and found that CsPGR5a played the dominant role in PGR5-dependent CEF. The results of yeast two-hybrid, biomolecular fluorescence complementation (BiFC), blue native PAGE, and coimmunoprecipitation (CoIP) assays showed that PGR5a interacted with PetC, Lhcb3, and PsaH. Furthermore, the intensity of the interactions was dynamic during state transitions, and the abundance of PGR5 attached to cyt b(6)f decreased during the transition from state 1 to state 2, which revealed that the function of PGR5a is related to the state transition. We proposed that PGR5 is a small mobile protein that functions when attached to protein complexes. Two PGR5s are present in some species of algae and higher plants, and CsPGR5a plays the dominant role in PGR5-dependent cyclic electron flow in cucumber. PGR5 is a small and mobile protein that functions when attached to protein complexes. In this study, the function of PGR5 was found to be partially related to the state transition.
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spelling pubmed-79334332021-03-19 The key cyclic electron flow protein PGR5 associates with cytochrome b(6)f, and its function is partially influenced by the LHCII state transition Wu, Xinyi Wu, Jianqiang Wang, Yu He, Meiwen He, Mingming Liu, Weikang Shu, Sheng Sun, Jin Guo, Shirong Hortic Res Article In plants and algae, PGR5-dependent cyclic electron flow (CEF) is an important regulator of acclimation to fluctuating environments, but how PGR5 participates in CEF is unclear. In this work, we analyzed two PGR5s in cucumber (Cucumis sativus L.) under different conditions and found that CsPGR5a played the dominant role in PGR5-dependent CEF. The results of yeast two-hybrid, biomolecular fluorescence complementation (BiFC), blue native PAGE, and coimmunoprecipitation (CoIP) assays showed that PGR5a interacted with PetC, Lhcb3, and PsaH. Furthermore, the intensity of the interactions was dynamic during state transitions, and the abundance of PGR5 attached to cyt b(6)f decreased during the transition from state 1 to state 2, which revealed that the function of PGR5a is related to the state transition. We proposed that PGR5 is a small mobile protein that functions when attached to protein complexes. Two PGR5s are present in some species of algae and higher plants, and CsPGR5a plays the dominant role in PGR5-dependent cyclic electron flow in cucumber. PGR5 is a small and mobile protein that functions when attached to protein complexes. In this study, the function of PGR5 was found to be partially related to the state transition. Nature Publishing Group UK 2021-03-04 /pmc/articles/PMC7933433/ /pubmed/33664242 http://dx.doi.org/10.1038/s41438-021-00460-y Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Wu, Xinyi
Wu, Jianqiang
Wang, Yu
He, Meiwen
He, Mingming
Liu, Weikang
Shu, Sheng
Sun, Jin
Guo, Shirong
The key cyclic electron flow protein PGR5 associates with cytochrome b(6)f, and its function is partially influenced by the LHCII state transition
title The key cyclic electron flow protein PGR5 associates with cytochrome b(6)f, and its function is partially influenced by the LHCII state transition
title_full The key cyclic electron flow protein PGR5 associates with cytochrome b(6)f, and its function is partially influenced by the LHCII state transition
title_fullStr The key cyclic electron flow protein PGR5 associates with cytochrome b(6)f, and its function is partially influenced by the LHCII state transition
title_full_unstemmed The key cyclic electron flow protein PGR5 associates with cytochrome b(6)f, and its function is partially influenced by the LHCII state transition
title_short The key cyclic electron flow protein PGR5 associates with cytochrome b(6)f, and its function is partially influenced by the LHCII state transition
title_sort key cyclic electron flow protein pgr5 associates with cytochrome b(6)f, and its function is partially influenced by the lhcii state transition
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7933433/
https://www.ncbi.nlm.nih.gov/pubmed/33664242
http://dx.doi.org/10.1038/s41438-021-00460-y
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