Cloning and Expression of HbHMAD1 from Hevea brasiliensis
Shi-Qing Peng
Abstract
Shi-Qing Peng
Abstract
The cDNA coding heavy-metal-associated domain protein,designated as HbHMAD1,was isolated from Hevea brasiliensis by rapid amplification of cDNA ends.HbHMAD1 consisted of a 453 bp open reading frame encoding 150 amino acids with molecular weight of 16.9 ku,a 78 bp 5'UTR and a 283 bp 3'UTR,.The deduced amino acid sequence of HbHMAD1 showed high identity of 85%,64%,63%,60% and 55% to those of the heavy-metal-associated domain protein from Ricinus communis,Arabidopsis thaliana and Zea mays,respectively.Semi-quantitative reverse transcription-polymerase chain reaction analysis revealed that HbHMAD1 was expressed more in the latex than in the barks,whereas little expression was detected in leaves and flower.
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The cDNA coding heavy-metal-associated domain protein,designated as HbHMAD1,was isolated from Hevea brasiliensis by rapid amplification of cDNA ends.HbHMAD1 consisted of a 453 bp open reading frame encoding 150 amino acids with molecular weight of 16.9 ku,a 78 bp 5'UTR and a 283 bp 3'UTR,.The deduced amino acid sequence of HbHMAD1 showed high identity of 85%,64%,63%,60% and 55% to those of the heavy-metal-associated domain protein from Ricinus communis,Arabidopsis thaliana and Zea mays,respectively.Semi-quantitative reverse transcription-polymerase chain reaction analysis revealed that HbHMAD1 was expressed more in the latex than in the barks,whereas little expression was detected in leaves and flower.
Key concepts: Hevea brasiliensis, Complementary DNA, Ricinus, Open reading frame, Biology, Cloning (programming), Rapid amplification of cDNA ends, Molecular biology