%0 Journal Article
%A LIU Guan-Jun
%A YANG Chuan-Ping*
%A ZHENG Lei
%T Cloning and Sequence Analysis of <em>rd</em>22 Gene from <em>Polygonum sibricum</em>
%D 2007
%R 10.7525/j.issn.1673-5102.2007.02.019
%J Bulletin of Botanical Research
%P 212-217
%V 27
%N 2
%X Using RACE (rapid amplification of cDNA ends) method, the full-length cDNA of dehydration-responsive protein RD22 was cloned from <em>Polygonum sibricum</em> treated with 3%NaHCO<sub>3</sub> solution for 48. The sequence analysis shows that the <em>rd</em>22 gene is 1 302 bp in length, including 59 bp of 5&prime;untranslated region, 25 bp of 3&prime;untranslated region and 1 218 bp of open reading frame (ORF).The <em>rd</em>22 gene encodes a protein of 405 amino acids. The C-terminal of the RD22 protein contains a conserved BURP domain, and the N-terminal contains 5 copies of a repetitive sequence of THV-VGKGGV-V. Signal peptide prediction shows the RD22 protein is a secretory protein, and has a signal peptide structure at the first 21 amino acids region. The amino acid sequence of RD22 prutein from <em>Polygonum sibricum</em> has a high homology with grape of 60%. This <em>rd</em>22 gene has been accepted by GenBank, and the accession number of gene sequence is DQ836050.
%U https://bbr.nefu.edu.cn/EN/10.7525/j.issn.1673-5102.2007.02.019