Abstract
A novel dehydrin gene designated as Cbcor29 was cloned from Capsella bursa-pastoris by rapid amplification of cDNA ends (RACE) and genome walker technique. The full-length cDNA of Cbcor29 was 1101 bp long with a 783 bp open reading frame (ORF), encoding a putative protein of 261 amino acids. Like other dehydrin proteins, CbCOR29 contained a high percentage of charged and polar amino acids, in which Cys and Trp amino acids were absent. In addition, the predicted CbCOR29 protein possesses three conserved repeats of the characterized Lys-rich domains (K-segments), and a Ser-rich domain (S-segment) prior to the first Lys-rich domain, which presented a typical SK3 structure of dehydrins. Analysis of Cbcor29 genomic DNA revealed that it contains 2 exons and 1 intron, which is a typical character of dehydrin genes. Subsequent bioinformatic analysis also showed that the sequence of CbCOR29 has high homology with other dehydrin proteins, especially with cor47 from Arabidopsis thaliana. Moreover, semi-quantitative RT-PCR revealed that the expression of Cbcor29 can be induced by exposure to drought, low temperature, NaCl, and exogenous ABA treatment. Our study led to the conclusion that the Cbcor29 gene is a new member of the dehydrin gene family and might exert functions in responsiveness to drought, cold, and salt in Capsella bursa-pastoris.
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Published in Russian in Molekulyarnaya Biologiya, 2006, Vol. 40, No. 1, pp. 52–60.
The article was submitted by the authors in English.
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Fan, Z., Wang, X. Isolation and characterization of a novel dehydrin gene from Capsella bursa-pastoris . Mol Biol 40, 43–50 (2006). https://doi.org/10.1134/S0026893306010080
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DOI: https://doi.org/10.1134/S0026893306010080