The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin

被引:65
作者
Mestres-Ortega, D [1 ]
Meyer, Y [1 ]
机构
[1] Univ Perpignan, Lab Physiol & Biol Mol Plantes, CNRS, UMR 5545, F-66860 Perpignan, France
关键词
Arabidopsis thaliana; chloroplast; evolution; redox; thioredoxin;
D O I
10.1016/S0378-1119(99)00448-5
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Screening of cDNA libraries at low stringency and complete sequencing of EST clones with homology to thioredoxins allowed us to characterize five new prokaryotic type Arabidopsis thaliana thioredoxins. All present N-terminal extensions with characteristics of transit peptides. Four are clustered in a phylogenetic tree with the chloroplastic thioredoxin m from red and green algae and higher plants, and their transit peptides have typical characteristics of chloroplastic transit peptides. One is clearly divergent and defines a new prokaryotic thioredoxin type that we have named thioredoxin x. Its transit peptide sequence presents characteristics of both chloroplastic and mitochondrial transit peptides. The five corresponding genes are expressed at different levels, but mostly in green tissues and in in-vitro cultivated cells. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:307 / 316
页数:10
相关论文
共 37 条
[1]   The complete genome sequence of Escherichia coli K-12 [J].
Blattner, FR ;
Plunkett, G ;
Bloch, CA ;
Perna, NT ;
Burland, V ;
Riley, M ;
ColladoVides, J ;
Glasner, JD ;
Rode, CK ;
Mayhew, GF ;
Gregor, J ;
Davis, NW ;
Kirkpatrick, HA ;
Goeden, MA ;
Rose, DJ ;
Mau, B ;
Shao, Y .
SCIENCE, 1997, 277 (5331) :1453-+
[2]   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
[3]   GENOMIC SEQUENCING [J].
CHURCH, GM ;
GILBERT, W .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (07) :1991-1995
[4]  
Doyle J. J., 1987, FOCUS, V19, P11, DOI DOI 10.2307/2419362
[5]   EXHAUSTIVE MATCHING OF THE ENTIRE PROTEIN-SEQUENCE DATABASE [J].
GONNET, GH ;
COHEN, MA ;
BENNER, SA .
SCIENCE, 1992, 256 (5062) :1443-1445
[6]   Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and ''APS reductase'' activity [J].
GutierrezMarcos, JF ;
Roberts, MA ;
Campbell, EI ;
Wray, JL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (23) :13377-13382
[7]   The cDNA sequence encoding bovine SP-22, a new defence system against reactive oxygen species in mitochondria [J].
Hiroi, T ;
Watabe, S ;
Takimoto, K ;
Yago, N ;
Yamamoto, Y ;
Takahashi, SY .
DNA SEQUENCE, 1996, 6 (04) :239-242
[8]  
ISHIWATARI Y, 1995, PLANTA, V195, P456, DOI 10.1007/BF00202605
[9]   Tansley review no 94 - Thioredoxins: Structure and function in plant cells [J].
Jacquot, JP ;
Lancelin, JM ;
Meyer, Y .
NEW PHYTOLOGIST, 1997, 136 (04) :543-570
[10]   High-yield expression of pea thioredoxin m and assessment of its efficiency in chloroplast fructose-1,6-bisphosphatase activation [J].
Jaramillo, JL ;
Chueca, A ;
Jacquot, JP ;
Hermoso, R ;
Lazaro, JJ ;
Sahrawy, M ;
Gorge, JL .
PLANT PHYSIOLOGY, 1997, 114 (04) :1169-1175