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

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...

Full description

Saved in:
Bibliographic Details
Published in:Gene 1999-11, Vol.240 (2), p.307-316
Main Authors: Mestres-Ortega, Dominique, Meyer, Yves
Format: Article
Language:English
Subjects:
Amino Acid Sequence
amino acid sequences
Arabidopsis - chemistry
Arabidopsis - genetics
Arabidopsis thaliana
Blotting, Southern
Chloroplast
complementary DNA
Databases, Factual
DNA, Complementary - chemistry
DNA, Complementary - genetics
DNA, Plant - analysis
DNA, Plant - genetics
Evolution
Expressed Sequence Tags
genbank/af095749
genbank/af095750
genbank/af095751
genbank/af095752
genbank/af095753
gene expression
Gene Expression Regulation, Plant
Gene Library
genes
genome
Genome, Plant
introns
messenger RNA
Molecular Sequence Data
nucleotide sequences
Phylogeny
Prokaryotic Cells - metabolism
Protein Isoforms - genetics
Redox
RNA, Plant - genetics
RNA, Plant - metabolism
Sequence Alignment
Sequence Analysis, DNA
Sequence Homology, Amino Acid
signal peptide
Southern blotting
Space life sciences
sulfur proteins
Thioredoxin
Thioredoxins - genetics
Tissue Distribution
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0378-1119
1879-0038
DOI:10.1016/S0378-1119(99)00448-5