The plant thioredoxin system

被引:241
作者
Gelhaye, E [1 ]
Rouhier, N [1 ]
Navrot, N [1 ]
Jacquot, JP [1 ]
机构
[1] Univ Henri Poincare, INRA,UMR 1136, Fac Sci, Unite Mixte Rech, F-54506 Vandoeuvre Les Nancy, France
关键词
disulfide bridge; redox regulation; thioredoxins; thiol reduction;
D O I
10.1007/s00018-004-4296-4
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
Thioredoxins are small proteins catalyzing thiol-disulfide interchange and are involved in the regulation of the redox environment of the cell. In plants, the thioredoxin system is particularly complex since at least 20 thioredoxin isoforms are found in the plant model Arabidopsis thaliana. Based upon primary sequence analysis and subcellular localization, thioredoxins can be classified into different groups and subgroups. Different pathways allowing thioredoxin reduction also coexist in the plant involving ferredoxin-thioredoxin reductase, thioredoxin reductases and the glutathione/glutaredoxin system. This review discusses the literature of plant thioredoxins with emphasis on recent findings in the field.
引用
收藏
页码:24 / 35
页数:12
相关论文
共 96 条
[1]   Exploring the molecular nature of alternative oxidase regulation and catalysis [J].
Affourtit, C ;
Albury, MSW ;
Crichton, PG ;
Moore, AL .
FEBS LETTERS, 2002, 510 (03) :121-126
[2]   The enolases of ice plant and Arabidopsis contain a potential disulphide and are redox sensitive [J].
Anderson, LE ;
Li, AD ;
Stevens, FJ .
PHYTOCHEMISTRY, 1998, 47 (05) :707-713
[3]   Physiological functions of thioredoxin and thioredoxin reductase [J].
Arnér, ESJ ;
Holmgren, A .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (20) :6102-6109
[4]   Reductive modification and nonreductive activation of purified spinach chloroplast NADP-dependent glyceraldehyde-3-phosphate dehydrogenase [J].
Baalmann, E ;
Backhausen, JE ;
Rak, C ;
Vetter, S ;
Scheibe, R .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1995, 324 (02) :201-208
[5]   Phloem sap proteins from Cucurbita maxima and Ricinus communis have the capacity to traffic cell to cell through plasmodesmata [J].
Balachandran, S ;
Xiang, Y ;
Schobert, C ;
Thompson, GA ;
Lucas, WJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (25) :14150-14155
[6]   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
[7]   Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria [J].
Balmer, Y ;
Vensel, WH ;
Tanaka, CK ;
Hurkman, WJ ;
Gelhaye, E ;
Rouhier, N ;
Jacquot, JP ;
Manieri, W ;
Schüurmann, P ;
Droux, M ;
Buchanan, BB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (08) :2642-2647
[8]   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
[9]   Plant thioredoxins: the multiplicity conundrum [J].
Baumann, U ;
Juttner, J .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2002, 59 (06) :1042-1057
[10]   Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana [J].
Bréhélin, C ;
Laloi, C ;
Setterdahl, AT ;
Knaff, DB ;
Meyer, Y .
PHOTOSYNTHESIS RESEARCH, 2004, 79 (03) :295-304