Isolation molecular characterisation and expression level of cytosolic heat-shock protein 90 (HSP90) genes of cryptocoryne ciliata a halophyte plant

Zairul Fazwan Zainordin, . and Cha Thye San, . and Aziz Ahmad, . Isolation molecular characterisation and expression level of cytosolic heat-shock protein 90 (HSP90) genes of cryptocoryne ciliata a halophyte plant. pp. 31-45. ISSN 2672-7226

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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Abstract

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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Item Type:	Article
AGROVOC Term:	Isolation
AGROVOC Term:	Halophytes
AGROVOC Term:	Molecular biology
AGROVOC Term:	Gene expression
AGROVOC Term:	Abiotic stress
AGROVOC Term:	Plant physiology
AGROVOC Term:	analysis
AGROVOC Term:	Experiments
AGROVOC Term:	Selection responses
AGROVOC Term:	Nucleotides
Depositing User:	Mr. AFANDI ABDUL MALEK
Last Modified:	24 Apr 2025 00:55
URI:	http://webagris.upm.edu.my/id/eprint/10326

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