[Back to Issue 5 ToC] [Back to Journal Contents] [Back to Biochemistry (Moscow) Home page]
[View Full Article] [Download Reprint (PDF)]

Identification and Differential Expression of Two Dehydrin cDNAs during Maturation of Jatropha curcas Seeds

S. A. Omar1,2, N. I. Elsheery3, H. M. Kalaji4*, M. K. H. Ebrahim5,6, S. Pietkiewicz4, C.-H. Lee7, S. I. Allakhverdiev8,9*, and Zeng-Fu Xu1*

1Key Laboratory of Tropical Plant Resource and Sustainable Use, Xishuangbanna Tropical Botanical Garden, Chinese Academy of Sciences, Menglun 666303, Yunnan, China; E-mail: zfxu@xtbg.ac.cn; zengfu.xu@gmail.com

2Genetic Department, Faculty of Agriculture, Tanta University, Egypt

3Agricultural Botany Department, Faculty of Agriculture, Tanta University, Tanta, Egypt

4Department of Plant Physiology, Warsaw University of Life Sciences SGGW, Nowoursynowska 159, 02-776 Warsaw, Poland; E-mail: hazem@kalaji.pl

5Biology Department, Faculty of Science, Taibah University, Almadinah Almunawwarah, KSA (Saudi Arabia)

6Botany Department, Faculty of Science, Tanta University, Tanta, Egypt

7Department of Molecular Biology, Pusan National University, Busan 609-735, Korea

8Institute of Plant Physiology, Russian Academy of Sciences, ul. Botanicheskaya 35, 127276 Moscow, Russia; E-mail: suleyman.allakhverdiev@gmail.com

9Institute of Basic Biological Problems, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

* To whom correspondence should be addressed.

Received January 25, 2013; Revision received February 1, 2013
Plant dehydrin proteins (DHNs) are known to be important for environmental stress tolerance and are involved in various developmental processes. Two full-length cDNAs JcDHN-1 and JcDHN-2 encoding two dehydrins from Jatropha curcas seeds were identified and characterized. JcDHN-1 is 764 bp long and contains an open reading frame of 528 bp. The deduced JcDHN-1 protein has 175 a.a. residues that form a 19.3-kDa polypeptide with a predicted isoelectric point (pI) of 6.41. JcDHN-2 is 855 bp long and contains an open reading frame of 441 bp. The deduced JcDHN-2 protein has 156 a.a. residues that form a 17.1-kDa polypeptide with a predicted pI of 7.09. JcDHN-1 is classified as type Y3SK2 and JcDHN-2 is classified as type Y2SK2 according to the YSK shorthand for structural classification of dehydrins. Homology analysis indicates that both JcDHN-1 and JcDHN-2 share identity with DHNs of other plants. Analysis of the conserved domain revealed that JcDHN-2 has glycoside hydrolase GH20 super-family activity. Quantitative real time PCR analysis for JcDHN-1 and JcDHN-2 expression during seed development showed increasing gene expression of both their transcript levels along with the natural dehydration process during seed development. A sharp increase in JcDHN-2 transcript level occurred in response to water content dropping from 42% in mature seeds to 12% in dry seeds. These results indicate that both JcDHNs have the potential to play a role in cell protection during dehydration occurring naturally during jatropha orthodox seed development.
KEY WORDS: dehydrin, Jatropha curcas, real time PCR, seed development

DOI: 10.1134/S0006297913050076