Cloning and molecular characterization of a copper chaperone gene (HbCCH1) from Hevea brasiliensis

摘要

The cDNA encoding?a?copper chaperone, designated as?HbCCH1, was isolated fromHevea brasiliensis.?HbCC1?was 589 bp long containing a 261 bp open reading frame encoding a putative protein of 86 amino acids, flanked by a 103 bp 5’UTR and a 225 bp 3’UTR. The predicted molecular mass of?HbCCH1?was?9.2 kDa, with an isoelectric point (pI) of 5.13.?The?HbCCH1?share the conserved N-terminal metal-binding domain (MXCXXC) and a lysine-rich C-terminus.?Reverse transcriptase polymerase chain reaction?(RT-PCR) analysis revealed that?HbCCH1?was constitutively expressed in all the tested tissues.?HbCCH1?transcripts were accumulated at relatively low levels in the?flower, bud and leaves,?while?HbCCH1?transcripts were accumulated at relatively high levels in the latex. The transcription of?HbCCH1?in the latex?was induced byjasmonate.