Malays. Appl. Biol. (2015) 44(1): 83-87
ISOLATION AND CHARACTERIZATION OF HEAT-SHOCK PROTEIN 90 (HSP90) SPECIFIC PROMOTER OF
Cryptocoryne ciliata
ZAIRUL-FAZWAN M. Z.1*, AZIZ A.1 and CHA T. S.2
1School of Science and Food Technology, Universiti Malaysia Terengganu,
21030 Kuala Terengganu, Terengganu, Malaysia
2School of Fundamental Science, Universiti Malaysia Terengganu,
21030 Kuala Terengganu, Terengganu, Malaysia
*E-mail: This e-mail address is being protected from spambots. You need JavaScript enabled to view it
ABSTRACT
Plants are equipped with various mechanisms for survival in extreme environments. Their ability to grow and adapt to extreme conditions such as high salinity, osmotic stress and ion toxicity is amazing. Heat-shock protein, particularly Hsp90, is one of the important parts of the chaperone machinery that involves in the protection of the structure and functions of cells and has a significant task in maintaining the cellular homeostasis. To further understand the functions of Hsp90 protein, a specific promoter for the CcHsp90-2 gene that encoded 700 amino acids (GenBank accession number: JN120021) was isolated from Cryptocoryne ciliata using the genome walker approach and later characterized. Based on the functional motif of the sequence (319 bp), the promoter consists of 13 cis-elements and stress factors such as light responsiveness, methyl jasmonate (MeJA) responsiveness, jasmonate-responsiveness (JERE) and many more. This finding gives further understanding on acquired stress tolerance of Hsp90 such as communication of specific Hsp/chaperones in a crowded cellular environment, the specific regulation of Hsp/chaperone molecules, participation in stress sensing, signal transduction and transcription activation of the stress gene.
Key words: Heat-shock protein 90, Chaperones, Cryptocoryne ciliata
