HCF243 Encodes a Chloroplast-Localized Protein Involved in the D1 Protein Stability of the Arabidopsis Photosystem II Complex

Numerous auxiliary nuclear factors have been identified to be involved in the dynamics of the photosystem II (PSII) complex. In this study, we characterized the high chlorophyll fluorescence243 (hcf243) mutant of Arabidopsis (Arabidopsis thaliana), shows higher chlorophyll fluorescence and is severe...

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Veröffentlicht in:Plant physiology (Bethesda) 2011-10, Vol.157 (2), p.608-619
Hauptverfasser: Zhang, Dongyuan, Zhou, Gongke, Liu, Bingbing, Kong, Yingzhen, Chen, Na, Qiu, Qiang, Yin, Hongju, An, Jiaxing, Zhang, Fang, Chen, Fan
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container_title Plant physiology (Bethesda)
container_volume 157
creator Zhang, Dongyuan
Zhou, Gongke
Liu, Bingbing
Kong, Yingzhen
Chen, Na
Qiu, Qiang
Yin, Hongju
An, Jiaxing
Zhang, Fang
Chen, Fan
description Numerous auxiliary nuclear factors have been identified to be involved in the dynamics of the photosystem II (PSII) complex. In this study, we characterized the high chlorophyll fluorescence243 (hcf243) mutant of Arabidopsis (Arabidopsis thaliana), shows higher chlorophyll fluorescence and is severely deficient in the accumulation of PSII supercomplexes compared with the wild type. The amount of core subunits was greatly decreased, while the outer antenna subunits and other subunits were hardly affected in hcf243. In vivo protein-labeling experiments indicated that the synthesis rate of both D1 and D2 proteins decreased severely in hcf243, whereas no change was found in the rate of other plastid-encoded proteins. Furthermore, the degradation rate of the PSII core subunit D1 protein is higher in hcf243 than in the wild type, and the assembly of PSII is retarded significantly in the hcf243 mutant. HCF243, a nuclear gene, encodes a chloroplast protein that interacts with the D1 protein. HCF243 homologs were identified in angiosperms with one or two copies but were not found in lower plants and prokaryotes. These results suggest that HCF243, which arose after the origin of the higher plants, may act as a cofactor to maintain the stability of D1 protein and to promote the subsequent assembly of the PSII complex.
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In this study, we characterized the high chlorophyll fluorescence243 (hcf243) mutant of Arabidopsis (Arabidopsis thaliana), shows higher chlorophyll fluorescence and is severely deficient in the accumulation of PSII supercomplexes compared with the wild type. The amount of core subunits was greatly decreased, while the outer antenna subunits and other subunits were hardly affected in hcf243. In vivo protein-labeling experiments indicated that the synthesis rate of both D1 and D2 proteins decreased severely in hcf243, whereas no change was found in the rate of other plastid-encoded proteins. Furthermore, the degradation rate of the PSII core subunit D1 protein is higher in hcf243 than in the wild type, and the assembly of PSII is retarded significantly in the hcf243 mutant. HCF243, a nuclear gene, encodes a chloroplast protein that interacts with the D1 protein. HCF243 homologs were identified in angiosperms with one or two copies but were not found in lower plants and prokaryotes. 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Psychology ; Genes ; Molecular Sequence Data ; Mutation ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Photosystem II ; Photosystem II Protein Complex - metabolism ; Plant cells ; Plant physiology and development ; Plants ; Plastids - genetics ; Protein Stability ; Proteins ; RNA, Messenger - metabolism ; Thylakoids ; Thylakoids - chemistry</subject><ispartof>Plant physiology (Bethesda), 2011-10, Vol.157 (2), p.608-619</ispartof><rights>2011 American Society of Plant Biologists</rights><rights>2015 INIST-CNRS</rights><rights>2011 American Society of Plant Biologists. 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In this study, we characterized the high chlorophyll fluorescence243 (hcf243) mutant of Arabidopsis (Arabidopsis thaliana), shows higher chlorophyll fluorescence and is severely deficient in the accumulation of PSII supercomplexes compared with the wild type. The amount of core subunits was greatly decreased, while the outer antenna subunits and other subunits were hardly affected in hcf243. In vivo protein-labeling experiments indicated that the synthesis rate of both D1 and D2 proteins decreased severely in hcf243, whereas no change was found in the rate of other plastid-encoded proteins. Furthermore, the degradation rate of the PSII core subunit D1 protein is higher in hcf243 than in the wild type, and the assembly of PSII is retarded significantly in the hcf243 mutant. HCF243, a nuclear gene, encodes a chloroplast protein that interacts with the D1 protein. HCF243 homologs were identified in angiosperms with one or two copies but were not found in lower plants and prokaryotes. These results suggest that HCF243, which arose after the origin of the higher plants, may act as a cofactor to maintain the stability of D1 protein and to promote the subsequent assembly of the PSII complex.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Biologists</pub><pmid>21862668</pmid><doi>10.1104/pp.111.183301</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record>
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subjects Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
BIOENERGETICS AND PHOTOSYNTHESIS
Biological and medical sciences
Chlorophyll - metabolism
Chlorophylls
Chloroplast Proteins - genetics
Chloroplast Proteins - metabolism
Chloroplasts
D1 protein
Fluorescence
Fundamental and applied biological sciences. Psychology
Genes
Molecular Sequence Data
Mutation
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Photosystem II
Photosystem II Protein Complex - metabolism
Plant cells
Plant physiology and development
Plants
Plastids - genetics
Protein Stability
Proteins
RNA, Messenger - metabolism
Thylakoids
Thylakoids - chemistry
title HCF243 Encodes a Chloroplast-Localized Protein Involved in the D1 Protein Stability of the Arabidopsis Photosystem II Complex
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