Cloning and molecular characterization of a copper chaperone gene (HbCCH1) from <i>Hevea brasiliensis</i>

Abstract

The cDNA encoding a copper chaperone, designated as HbCCH1, was isolated from Hevea 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 metalbinding 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 by jasmonate.

Key words: Copper chaperone, Hevea brasiliensis, latex.