Isolation, molecular characterisation and expression level of cytosolic heat-shock protein 90 (HSP90) genes of cryptocoryne ciliata, a halophyte plant
2021
Zairul Fazwan Zainordin | Cha, Thye San | Aziz Ahmad
Heat-shock protein 90 (HSP90) assembly in the cell involves protein-folding, as well as plant growth and response to environmental stimuli. Little is known regarding the sequence and function of HSP90s in halophytes plants. In the present study, a partial cDNA sequence of CcHsp90-1 and, a full-length cDNA of CcHsp90-2 from Cryptocoryne ciliata were cloned and sequenced. The full-length CcHsp90-2 cDNA sequence, containing 2465 base pairs, encoding a protein of 700 amino acids. The molecular mass of CcHsp90-2 protein was estimated at 79.95 kDa, which is 89 to 94 % homology to plant HSP90 protein. The protein possesses five-conserved amino acid signature sequence motifs characteristic of the HSP90 family and a C-terminus MEEVD penta-peptide characteristic, encoded by HSP90A group, which is mainly expressed in the cytosol. The predicted quaternary architecture structure for CcHsp90-2 protein generated through molecular modeling was globally akin to yeast HSP90. The CcHsp90s gene expression analyses in leaves of C. ciliata towards salinity treatment using the qRT-PCR analysis showed that both, CcHsp90-1 and CcHsp90-2 genes were significantly up-regulated with an optimum expression of 5.66 and 8.94-fold, respectively. It is suggested that few HSP90 isoforms might be synergistically exerted in regulating the salinity stress by C. ciliata.
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