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ApcD is necessary for efficient energy transfer from phycobilisomes to photosystem I and helps to prevent photoinhibition in the cyanobacterium Synechococcus sp PCC 7002
Dong, Chunxia1; Tang, Aihui1; Zhao, Jindong1,2; Mullineaux, Conrad W.3; Shen, Gaozhong4; Bryant, Donald A.4; Zhao, JD, Peking Univ, Coll Life Sci, State Key Lab Prot & Plant Genet Engn, Beijing 100871, Peoples R China
2009-09-01
Source PublicationBIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
ISSN0005-2728
Volume1787Issue:9Pages:1122-1128
AbstractPhyrobilisomes (PBS) are the major light-harvesting, protein-pigment complexes in cyanobacteria and red algae. PBS absorb and transfer light energy to photosystem (PS) II as well as PS I, and the distribution of light energy from PBS to the two photosystems is regulated by light conditions through a mechanism known as state transitions. In this study the quantum efficiency of excitation energy transfer from PBS to PS I in the cyanobacterium Synechococcus sp. PCC 7002 was determined, and the results showed that energy transfer from PBS to PS I is extremely efficient. The results further demonstrated that energy transfer from PBS to PS I occurred directly and that efficient energy transfer was dependent upon the allophycocyanin-B alpha subunit, ApcD. In the absence of ApcD, cells were unable to perform state transitions and were trapped in state 1. Action spectra showed that light energy transfer from PBS to PS I was severely impaired in the absence of ApcD. An apcD mutant grew more slowly than the wild type in light preferentially absorbed by phyrobiliproteins and was more sensitive to high light intensity. On the other hand, a mutant lacking ApcF, which is required for efficient energy transfer from PBS to PS II, showed greater resistance to high light treatment. Therefore, state transitions in cyanobacteria have two roles: (1) they regulate light energy distribution between the two photosystems; and (2) they help to protect cells from the effects of light energy excess at high light intensities. (C) 2009 Elsevier B.V. All rights reserved.; Phyrobilisomes (PBS) are the major light-harvesting, protein-pigment complexes in cyanobacteria and red algae. PBS absorb and transfer light energy to photosystem (PS) II as well as PS I, and the distribution of light energy from PBS to the two photosystems is regulated by light conditions through a mechanism known as state transitions. In this study the quantum efficiency of excitation energy transfer from PBS to PS I in the cyanobacterium Synechococcus sp. PCC 7002 was determined, and the results showed that energy transfer from PBS to PS I is extremely efficient. The results further demonstrated that energy transfer from PBS to PS I occurred directly and that efficient energy transfer was dependent upon the allophycocyanin-B alpha subunit, ApcD. In the absence of ApcD, cells were unable to perform state transitions and were trapped in state 1. Action spectra showed that light energy transfer from PBS to PS I was severely impaired in the absence of ApcD. An apcD mutant grew more slowly than the wild type in light preferentially absorbed by phyrobiliproteins and was more sensitive to high light intensity. On the other hand, a mutant lacking ApcF, which is required for efficient energy transfer from PBS to PS II, showed greater resistance to high light treatment. Therefore, state transitions in cyanobacteria have two roles: (1) they regulate light energy distribution between the two photosystems; and (2) they help to protect cells from the effects of light energy excess at high light intensities. (C) 2009 Elsevier B.V. All rights reserved.
SubtypeArticle
KeywordCyanobacteria Phycobilisome Photosynthesis State Transition Photosystem i Photosystem Ii Synechococcus Sp Pcc 7002
Department[Dong, Chunxia; Tang, Aihui; Zhao, Jindong] Peking Univ, Coll Life Sci, State Key Lab Prot & Plant Genet Engn, Beijing 100871, Peoples R China; [Zhao, Jindong] Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Peoples R China; [Mullineaux, Conrad W.] Queen Mary Univ London, Sch Biol Sci, London E1 4NS, England; [Shen, Gaozhong; Bryant, Donald A.] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
Subject AreaBiochemistry & Molecular Biology ; Biophysics
DOI10.1016/j.bbabio.2009.04.007
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Funding OrganizationThe National Natural Science Foundation of China [30230040]; Ministry of Science and Technology of China [2009CB11850]; Wellcome Trust ; Biotechnology and Biological Sciences Research Council ; U.S. National Science Foundation [MCB-0519743] ; The National Natural Science Foundation of China [30230040]; Ministry of Science and Technology of China [2009CB11850]; Wellcome Trust ; Biotechnology and Biological Sciences Research Council ; U.S. National Science Foundation [MCB-0519743] ; The National Natural Science Foundation of China [30230040]; Ministry of Science and Technology of China [2009CB11850]; Wellcome Trust ; Biotechnology and Biological Sciences Research Council ; U.S. National Science Foundation [MCB-0519743] ; The National Natural Science Foundation of China [30230040]; Ministry of Science and Technology of China [2009CB11850]; Wellcome Trust ; Biotechnology and Biological Sciences Research Council ; U.S. National Science Foundation [MCB-0519743]
Indexed BySCI
Language英语
WOS Research AreaBiochemistry & Molecular Biology ; Biophysics
WOS SubjectBiochemistry & Molecular Biology ; Biophysics
WOS IDWOS:000267926900005
WOS KeywordSTATE TRANSITIONS ; EXCITATION-ENERGY ; SP PCC-7002 ; PHOTOSYNTHETIC APPARATUS ; THYLAKOID MEMBRANES ; ANACYSTIS-NIDULANS ; LIGHT ; MUTANT ; SYNECHOCYSTIS ; FLUORESCENCE
Funding OrganizationThe National Natural Science Foundation of China [30230040]; Ministry of Science and Technology of China [2009CB11850]; Wellcome Trust ; Biotechnology and Biological Sciences Research Council ; U.S. National Science Foundation [MCB-0519743] ; The National Natural Science Foundation of China [30230040]; Ministry of Science and Technology of China [2009CB11850]; Wellcome Trust ; Biotechnology and Biological Sciences Research Council ; U.S. National Science Foundation [MCB-0519743] ; The National Natural Science Foundation of China [30230040]; Ministry of Science and Technology of China [2009CB11850]; Wellcome Trust ; Biotechnology and Biological Sciences Research Council ; U.S. National Science Foundation [MCB-0519743] ; The National Natural Science Foundation of China [30230040]; Ministry of Science and Technology of China [2009CB11850]; Wellcome Trust ; Biotechnology and Biological Sciences Research Council ; U.S. National Science Foundation [MCB-0519743]
Citation statistics
Cited Times:59[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/152342/7660
Collection期刊论文
Corresponding AuthorZhao, JD, Peking Univ, Coll Life Sci, State Key Lab Prot & Plant Genet Engn, Beijing 100871, Peoples R China
Affiliation1.Peking Univ, Coll Life Sci, State Key Lab Prot & Plant Genet Engn, Beijing 100871, Peoples R China
2.Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Peoples R China
3.Queen Mary Univ London, Sch Biol Sci, London E1 4NS, England
4.Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
Recommended Citation
GB/T 7714
Dong, Chunxia,Tang, Aihui,Zhao, Jindong,et al. ApcD is necessary for efficient energy transfer from phycobilisomes to photosystem I and helps to prevent photoinhibition in the cyanobacterium Synechococcus sp PCC 7002[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,2009,1787(9):1122-1128.
APA Dong, Chunxia.,Tang, Aihui.,Zhao, Jindong.,Mullineaux, Conrad W..,Shen, Gaozhong.,...&Zhao, JD, Peking Univ, Coll Life Sci, State Key Lab Prot & Plant Genet Engn, Beijing 100871, Peoples R China.(2009).ApcD is necessary for efficient energy transfer from phycobilisomes to photosystem I and helps to prevent photoinhibition in the cyanobacterium Synechococcus sp PCC 7002.BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,1787(9),1122-1128.
MLA Dong, Chunxia,et al."ApcD is necessary for efficient energy transfer from phycobilisomes to photosystem I and helps to prevent photoinhibition in the cyanobacterium Synechococcus sp PCC 7002".BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1787.9(2009):1122-1128.
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