CcdA Is a Thylakoid Membrane Protein Required for the Transfer of Reducing Equivalents from Stroma to Thylakoid Lumen in the Higher Plant Chloroplast

被引:50
作者
Motohashi, Ken [1 ,2 ]
Hisabori, Toru [2 ]
机构
[1] Kyoto Sangyo Univ, Fac Life Sci, Dept Bioresource & Environm Sci, Kyoto 6038555, Japan
[2] Tokyo Inst Technol, Chem Resources Lab, Yokohama, Kanagawa 227, Japan
基金
日本学术振兴会;
关键词
DISULFIDE BOND FORMATION; CYTOCHROME B(6)F COMPLEX; OUTER ENVELOPE MEMBRANE; ARABIDOPSIS-THALIANA; PLASTIDIAL THIOREDOXINS; REDUCTIVE ACTIVATION; ELECTRON-TRANSFER; ESCHERICHIA-COLI; TARGET PROTEINS; PHOTOSYSTEM-II;
D O I
10.1089/ars.2010.3138
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In order to transfer reducing equivalents into the thylakoid lumen, a specific thylakoid membrane transfer system is suggested that mediates the disulfide bond reduction of proteins in the thylakoid lumen of higher plant chloroplasts. In this system, although stromal thioredoxin can supply the reducing equivalents to a thioredoxin-like protein HCF164 in the thylakoid lumen, a mediator protein for electron transfer in the thylakoid membranes is proposed to be required to link the two suborganellar compartments. CcdA is a candidate protein as a component for this transfer system since CcdA- and HCF164-deficient mutants in Arabidopsis thaliana show the same phenotype. We now show that CcdA is localized in the thylakoid membrane and that its redox state, as well as that of HCF164, is modulated in thylakoids by stromal m-type thioredoxin. Our results strongly suggest that CcdA may act as a mediator in thylakoid membranes by transferring reducing equivalents from the stromal to the lumenal side of the thylakoid membrane in chloroplasts. Antioxid. Redox Signal. 13, 1169-1176.
引用
收藏
页码:1169 / 1176
页数:8
相关论文
共 57 条
[1]   Two types of MGDG synthase genes, found widely in both 16:3 and 18:3 plants, differentially mediate galactolipid syntheses in photosynthetic and nonphotosynthetic tissues in Arabidopsis thaliana [J].
Awai, K ;
Maréchal, E ;
Block, MA ;
Brun, D ;
Masuda, T ;
Shimada, H ;
Takamiya, K ;
Ohta, H ;
Joyard, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (19) :10960-10965
[2]   Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin [J].
Ballicora, MA ;
Frueauf, JB ;
Fu, YB ;
Schürmann, P ;
Preiss, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (02) :1315-1320
[3]   Proteomics gives insight into the regulatory function of chloroplast thioredoxins [J].
Balmer, Y ;
Koller, A ;
del Val, G ;
Manieri, W ;
Schürmann, P ;
Buchanan, BB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (01) :370-375
[4]   PURIFICATION AND CHARACTERIZATION OF E37, A MAJOR CHLOROPLAST ENVELOPE PROTEIN [J].
BLOCK, MA ;
JOYARD, J ;
DOUCE, R .
FEBS LETTERS, 1991, 287 (1-2) :167-170
[5]  
BRANDES HK, 1993, J BIOL CHEM, V268, P18411
[6]   Redox regulation: A broadening horizon [J].
Buchanan, BB ;
Balmer, Y .
ANNUAL REVIEW OF PLANT BIOLOGY, 2005, 56 :187-220
[7]   ROLE OF LIGHT IN THE REGULATION OF CHLOROPLAST ENZYMES [J].
BUCHANAN, BB .
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1980, 31 :341-374
[8]   PHOTOSYNTHETIC REGULATORY PROTEIN FOUND IN ANIMAL AND BACTERIAL-CELLS [J].
BUCHANAN, BB ;
WOLOSIUK, RA .
NATURE, 1976, 264 (5587) :669-670
[9]   Preparation and functional characterization of thylakoids from Arabidopsis thaliana [J].
Casazza, AP ;
Tarantino, D ;
Soave, C .
PHOTOSYNTHESIS RESEARCH, 2001, 68 (02) :175-180
[10]  
CLANCEY CJ, 1987, J BIOL CHEM, V262, P13545