Isolation and molecular characterization of a cax gene from Capsella bursa-pastoris.
A new cation exchangers (CAXs) gene was cloned and characterized from Capsella bursa-pastoris by rapid amplification of cDNA ends (RACE). The full-length cDNA sequence of cax from C. bursa-pastoris (designated as Cbcax51) was 1754 bp containing a 1398 bp open reading frame encoding a polypeptide of 466 amino-acid residues with a calculated molecular mass of 50.5 kDa and an isoelectric point of 5.69. The predicted CbCAX51 contained an IMP dehydrogenase/GMP reductase domain, two Na+/Ca2+ exchanger protein domains. Comparative and bioinformatics analyses revealed that CbCAX51 showed extensive homology with CAX from other plant species. The expression analysis by different treatments indicated that Cbcax51 could be activated by cold triggering and was related to the cold acclimation process, but its expression is regulated negatively by drought and not affected by ABA or salt.
Lin
Juan
J
State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan-SJTU-Nottingham Plant Biotechnology R&D Center, Fudan University, Shanghai, People's Republic of China. linjuan@fudan.edu.cn
Zhang
Wen
W
Shi
Mingzhu
M
Wang
Xinglong
X
Sun
Xiaofen
X
Tang
Kexuan
K
D000595:Amino Acid Sequence; D017920:Antiporters / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D029687:Capsella / Q000235:genetics* / Q000378:metabolism; D019295:Computational Biology; D017343:Genes, Plant; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
D017920:Antiporters; D010940:Plant Proteins