Isolation and Characterization of Calmodulin 2 (CICAM2) Gene from Codonopsis lanceolata
- Lee, Kang In, Jun-Gyo Yu, Chang-Yeon Min, Byung-Hoon Chung, Ill-Min Kim, Se-Young Kim, Yeong-Chae Yang, Deok-Chun
- Plant Resources
- Vol.7 No.3
- 174 - 180 (7 pages)
Calmodulin, a Ca^2+-binding protein, has no enzyme activity. It combines with Ca^2+ and makes variable proteins to an active form. Calmodulin 2 is a ubiquitous protein in plants. To investigate the defense mechanism against various stresses, a clone encoding a calmodulin 2 protein was isolated from a cDNA library prepared from taproot mRNAs of Codonopsis lanceolata. The cDNA, designated CICAM2, is 719 nucleotides long and has an open reading frame of 450 bp with a deduced amino acid sequence of 149 residues. The deduced amino acid sequence of CICAM2 showed a high similarity with calmodulins of P. x hybrida (P27163) 97%, N. tabacum (BAB61908) 97%, S. tuberosum (AAA74405) 96%, Z. mays (CAA74307) 92%, C. richardii (AF510075) 93%, M. truncatula (AAM81203) 91%, and G. max (P62163) 91%. The transcriptional expression of the CICAM2 gene, was gradually increased by the CaCl₂ treatment. Whereas its expression And it was gradually decreased in the cold stress treatment.ent.
MATERIAL AND METHODS
RESULT AND DISCUSSION