Triose phosphate translocator (TPT) is located in the inner membrane of plant chloroplasts. It catalyzes the counter exchange of those phosphate/3-phosphoglycerate and phosphate. To obtain the basic information on the...Triose phosphate translocator (TPT) is located in the inner membrane of plant chloroplasts. It catalyzes the counter exchange of those phosphate/3-phosphoglycerate and phosphate. To obtain the basic information on the structure-function relation, a cDNA encoding the complete precursor of the triose phosphate translocator has been isolated from wheat (Triticum aestivum L.) by RACE ( rapid amplification of cDNA ends) strategies. The wheat TPT cDNA encodes a precursor protein of 402 amino acid residues with a deduced molecular weight of 43 kD. A putative processing site between Ala-78 and Ala-79 of the precursor protein is suggested by comparison with those of the TPTs from spinach (Spinacia oleracea Mill.) and maize (Zea mays L.). The mature part of wheat TPT consists of 324 amino acid with a molecular weight of 35 kD, which share 89% identity with maize TPT. The amino acids Lys-274 and Arg-275 (mature protein) which is regarded as the substrate-binding site, are both conserved in plant TPTs. The gene expression analysis for leaves, coleoptiles, roots and seeds of wheat showed that the TPT transcript was only detectable in leaves and coleoptiles. No apparent expression signal was detected in the roots and seeds. This indicated that the expression of wheat TPT might be restricted to green tissues.展开更多
文摘Triose phosphate translocator (TPT) is located in the inner membrane of plant chloroplasts. It catalyzes the counter exchange of those phosphate/3-phosphoglycerate and phosphate. To obtain the basic information on the structure-function relation, a cDNA encoding the complete precursor of the triose phosphate translocator has been isolated from wheat (Triticum aestivum L.) by RACE ( rapid amplification of cDNA ends) strategies. The wheat TPT cDNA encodes a precursor protein of 402 amino acid residues with a deduced molecular weight of 43 kD. A putative processing site between Ala-78 and Ala-79 of the precursor protein is suggested by comparison with those of the TPTs from spinach (Spinacia oleracea Mill.) and maize (Zea mays L.). The mature part of wheat TPT consists of 324 amino acid with a molecular weight of 35 kD, which share 89% identity with maize TPT. The amino acids Lys-274 and Arg-275 (mature protein) which is regarded as the substrate-binding site, are both conserved in plant TPTs. The gene expression analysis for leaves, coleoptiles, roots and seeds of wheat showed that the TPT transcript was only detectable in leaves and coleoptiles. No apparent expression signal was detected in the roots and seeds. This indicated that the expression of wheat TPT might be restricted to green tissues.
