Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase–thioredoxin h system from wheat
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منابع مشابه
Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase-thioredoxin h system from wheat.
Thioredoxins h are ubiquitous proteins reduced by NADPH- thioredoxin reductase (NTR). They are able to reduce disulphides in target proteins. In monocots, thioredoxins h accumulate at high level in seeds and show a predominant localization in the nucleus of seed cells. These results suggest that the NTR-thioredoxin h system probably plays an important role in seed physiology. To date, the study...
متن کاملCloning and characterization of thioredoxin h in the three-pistil line of common wheat.
Thioredoxin h (Trxh) is a ubiquitous protein that reduces disulfides in target proteins, and is itself reduced by NADPH-thioredoxin reductase. In the current study, the complementary DNA sequence and the genomic sequence of the three-pistil (TP) line of common wheat (Triticum aestivum L.) were obtained from spikes through reverse transcription-polymerase chain reaction (RT-PCR) and touchdown-PC...
متن کاملNADPH-Dependent Thioredoxin Reductase and a New Thioredoxin from Wheat
An albumin fraction extracted from wheat flour contains thioredoxin reductase (Mr = 65,000) and a heat-stable thioredoxin (Mr = 15,000) which are separated on DEAE cellulose and further purified by gel filtration. W heat thioredoxin stimulates E. coli ribonucleotide reductase but not chloroplast fructose-bis-phosphatase. The enzyme is NADPH-dependent (Km = 3.2 X 10 -6 m) . In presence of the th...
متن کاملThe thioredoxin h system of higher plants.
In plants, thioredoxins h are encoded by a multigenic family of genes (eight in Arabidopsis thaliana, at least five in Populus sp.). The multiplicity of these isoforms raises the question of their specificity. This review focuses on thioredoxins h in two plant models: Arabidopsis and poplar. Thioredoxins h can be divided into three different subgroups according to the analysis of their primary ...
متن کاملCharacterization of a thioredoxin-thioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima.
A thioredoxin reductase and a thioredoxin were purified to homogeneity from a cell extract of Thermotoga maritima. The thioredoxin reductase was a homodimeric flavin adenine dinucleotide (FAD)-containing protein with a subunit of 37 kDa estimated using SDS-PAGE, which was identified to be TM0869. The amino acid sequence of the enzyme showed high identities and similarities to those of typical b...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2002
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20020103