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Arabidopsis thaliana PGR7 Encodes a Conserved Chloroplast Protein That Is Necessary for Efficient Photosynthetic Electron Transport

A significant fraction of a plant's nuclear genome encodes chloroplast-targeted proteins, many of which are devoted to the assembly and function of the photosynthetic apparatus. Using digital video imaging of chlorophyll fluorescence, we isolated proton gradient regulation 7 (pgr7) as an Arabid...

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Autores principales: Jung, Hou-Sung, Okegawa, Yuki, Shih, Patrick M., Kellogg, Elizabeth, Abdel-Ghany, Salah E., Pilon, Marinus, Sjölander, Kimmen, Shikanai, Toshiharu, Niyogi, Krishna K.
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2908147/
https://www.ncbi.nlm.nih.gov/pubmed/20657737
http://dx.doi.org/10.1371/journal.pone.0011688
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author Jung, Hou-Sung
Okegawa, Yuki
Shih, Patrick M.
Kellogg, Elizabeth
Abdel-Ghany, Salah E.
Pilon, Marinus
Sjölander, Kimmen
Shikanai, Toshiharu
Niyogi, Krishna K.
author_facet Jung, Hou-Sung
Okegawa, Yuki
Shih, Patrick M.
Kellogg, Elizabeth
Abdel-Ghany, Salah E.
Pilon, Marinus
Sjölander, Kimmen
Shikanai, Toshiharu
Niyogi, Krishna K.
author_sort Jung, Hou-Sung
collection PubMed
description A significant fraction of a plant's nuclear genome encodes chloroplast-targeted proteins, many of which are devoted to the assembly and function of the photosynthetic apparatus. Using digital video imaging of chlorophyll fluorescence, we isolated proton gradient regulation 7 (pgr7) as an Arabidopsis thaliana mutant with low nonphotochemical quenching of chlorophyll fluorescence (NPQ). In pgr7, the xanthophyll cycle and the PSBS gene product, previously identified NPQ factors, were still functional, but the efficiency of photosynthetic electron transport was lower than in the wild type. The pgr7 mutant was also smaller in size and had lower chlorophyll content than the wild type in optimal growth conditions. Positional cloning located the pgr7 mutation in the At3g21200 (PGR7) gene, which was predicted to encode a chloroplast protein of unknown function. Chloroplast targeting of PGR7 was confirmed by transient expression of a GFP fusion protein and by stable expression and subcellular localization of an epitope-tagged version of PGR7. Bioinformatic analyses revealed that the PGR7 protein has two domains that are conserved in plants, algae, and bacteria, and the N-terminal domain is predicted to bind a cofactor such as FMN. Thus, we identified PGR7 as a novel, conserved nuclear gene that is necessary for efficient photosynthetic electron transport in chloroplasts of Arabidopsis.
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spelling pubmed-29081472010-07-23 Arabidopsis thaliana PGR7 Encodes a Conserved Chloroplast Protein That Is Necessary for Efficient Photosynthetic Electron Transport Jung, Hou-Sung Okegawa, Yuki Shih, Patrick M. Kellogg, Elizabeth Abdel-Ghany, Salah E. Pilon, Marinus Sjölander, Kimmen Shikanai, Toshiharu Niyogi, Krishna K. PLoS One Research Article A significant fraction of a plant's nuclear genome encodes chloroplast-targeted proteins, many of which are devoted to the assembly and function of the photosynthetic apparatus. Using digital video imaging of chlorophyll fluorescence, we isolated proton gradient regulation 7 (pgr7) as an Arabidopsis thaliana mutant with low nonphotochemical quenching of chlorophyll fluorescence (NPQ). In pgr7, the xanthophyll cycle and the PSBS gene product, previously identified NPQ factors, were still functional, but the efficiency of photosynthetic electron transport was lower than in the wild type. The pgr7 mutant was also smaller in size and had lower chlorophyll content than the wild type in optimal growth conditions. Positional cloning located the pgr7 mutation in the At3g21200 (PGR7) gene, which was predicted to encode a chloroplast protein of unknown function. Chloroplast targeting of PGR7 was confirmed by transient expression of a GFP fusion protein and by stable expression and subcellular localization of an epitope-tagged version of PGR7. Bioinformatic analyses revealed that the PGR7 protein has two domains that are conserved in plants, algae, and bacteria, and the N-terminal domain is predicted to bind a cofactor such as FMN. Thus, we identified PGR7 as a novel, conserved nuclear gene that is necessary for efficient photosynthetic electron transport in chloroplasts of Arabidopsis. Public Library of Science 2010-07-21 /pmc/articles/PMC2908147/ /pubmed/20657737 http://dx.doi.org/10.1371/journal.pone.0011688 Text en Jung et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Jung, Hou-Sung
Okegawa, Yuki
Shih, Patrick M.
Kellogg, Elizabeth
Abdel-Ghany, Salah E.
Pilon, Marinus
Sjölander, Kimmen
Shikanai, Toshiharu
Niyogi, Krishna K.
Arabidopsis thaliana PGR7 Encodes a Conserved Chloroplast Protein That Is Necessary for Efficient Photosynthetic Electron Transport
title Arabidopsis thaliana PGR7 Encodes a Conserved Chloroplast Protein That Is Necessary for Efficient Photosynthetic Electron Transport
title_full Arabidopsis thaliana PGR7 Encodes a Conserved Chloroplast Protein That Is Necessary for Efficient Photosynthetic Electron Transport
title_fullStr Arabidopsis thaliana PGR7 Encodes a Conserved Chloroplast Protein That Is Necessary for Efficient Photosynthetic Electron Transport
title_full_unstemmed Arabidopsis thaliana PGR7 Encodes a Conserved Chloroplast Protein That Is Necessary for Efficient Photosynthetic Electron Transport
title_short Arabidopsis thaliana PGR7 Encodes a Conserved Chloroplast Protein That Is Necessary for Efficient Photosynthetic Electron Transport
title_sort arabidopsis thaliana pgr7 encodes a conserved chloroplast protein that is necessary for efficient photosynthetic electron transport
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2908147/
https://www.ncbi.nlm.nih.gov/pubmed/20657737
http://dx.doi.org/10.1371/journal.pone.0011688
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