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The function of LHCBM4/6/8 antenna proteins in Chlamydomonas reinhardtii
In eukaryotic autotrophs, photosystems are composed of a core moiety, hosting charge separation and electron transport reactions, and an antenna system, enhancing light harvesting and photoprotection. In Chlamydomonas reinhardtii, the major antenna of PSII is a heterogeneous trimeric complex made up...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5441897/ https://www.ncbi.nlm.nih.gov/pubmed/28007953 http://dx.doi.org/10.1093/jxb/erw462 |
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author | Girolomoni, Laura Ferrante, Paola Berteotti, Silvia Giuliano, Giovanni Bassi, Roberto Ballottari, Matteo |
author_facet | Girolomoni, Laura Ferrante, Paola Berteotti, Silvia Giuliano, Giovanni Bassi, Roberto Ballottari, Matteo |
author_sort | Girolomoni, Laura |
collection | PubMed |
description | In eukaryotic autotrophs, photosystems are composed of a core moiety, hosting charge separation and electron transport reactions, and an antenna system, enhancing light harvesting and photoprotection. In Chlamydomonas reinhardtii, the major antenna of PSII is a heterogeneous trimeric complex made up of LHCBM1–LHCBM9 subunits. Despite high similarity, specific functions have been reported for several members including LHCBM1, 2, 7, and 9. In this work, we analyzed the function of LHCBM4 and LHCBM6 gene products in vitro by synthesizing recombinant apoproteins from individual sequences and refolding them with pigments. Additionally, we characterized knock-down strains in vivo for LHCBM4/6/8 genes. We show that LHCBM4/6/8 subunits could be found as a component of PSII supercomplexes with different sizes, although the largest pool was free in the membranes and poorly connected to PSII. Impaired accumulation of LHCBM4/6/8 caused a decreased LHCII content per PSII and a reduction in the amplitude of state 1–state 2 transitions. In addition, the reduction of LHCBM4/6/8 subunits caused a significant reduction of the Non-photochemical quenching activity and in the level of photoprotection. |
format | Online Article Text |
id | pubmed-5441897 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-54418972017-05-30 The function of LHCBM4/6/8 antenna proteins in Chlamydomonas reinhardtii Girolomoni, Laura Ferrante, Paola Berteotti, Silvia Giuliano, Giovanni Bassi, Roberto Ballottari, Matteo J Exp Bot Research Paper In eukaryotic autotrophs, photosystems are composed of a core moiety, hosting charge separation and electron transport reactions, and an antenna system, enhancing light harvesting and photoprotection. In Chlamydomonas reinhardtii, the major antenna of PSII is a heterogeneous trimeric complex made up of LHCBM1–LHCBM9 subunits. Despite high similarity, specific functions have been reported for several members including LHCBM1, 2, 7, and 9. In this work, we analyzed the function of LHCBM4 and LHCBM6 gene products in vitro by synthesizing recombinant apoproteins from individual sequences and refolding them with pigments. Additionally, we characterized knock-down strains in vivo for LHCBM4/6/8 genes. We show that LHCBM4/6/8 subunits could be found as a component of PSII supercomplexes with different sizes, although the largest pool was free in the membranes and poorly connected to PSII. Impaired accumulation of LHCBM4/6/8 caused a decreased LHCII content per PSII and a reduction in the amplitude of state 1–state 2 transitions. In addition, the reduction of LHCBM4/6/8 subunits caused a significant reduction of the Non-photochemical quenching activity and in the level of photoprotection. Oxford University Press 2017-01-01 2016-12-22 /pmc/articles/PMC5441897/ /pubmed/28007953 http://dx.doi.org/10.1093/jxb/erw462 Text en © The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/4.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Girolomoni, Laura Ferrante, Paola Berteotti, Silvia Giuliano, Giovanni Bassi, Roberto Ballottari, Matteo The function of LHCBM4/6/8 antenna proteins in Chlamydomonas reinhardtii |
title | The function of LHCBM4/6/8 antenna proteins in Chlamydomonas reinhardtii |
title_full | The function of LHCBM4/6/8 antenna proteins in Chlamydomonas reinhardtii |
title_fullStr | The function of LHCBM4/6/8 antenna proteins in Chlamydomonas reinhardtii |
title_full_unstemmed | The function of LHCBM4/6/8 antenna proteins in Chlamydomonas reinhardtii |
title_short | The function of LHCBM4/6/8 antenna proteins in Chlamydomonas reinhardtii |
title_sort | function of lhcbm4/6/8 antenna proteins in chlamydomonas reinhardtii |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5441897/ https://www.ncbi.nlm.nih.gov/pubmed/28007953 http://dx.doi.org/10.1093/jxb/erw462 |
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