%0 Journal Article
%T Cloning and sequence analysis of a new cathepsin L-like cysteine proteinase gene from Ditylenchus destructor<br>马铃薯腐烂茎线虫L 型半胱氨酸蛋白酶新基因(Dd-cpl-1) 的克隆与序列分析
%A Gaofeng Wang
%A Deliang Peng
%A Jianhua Sun
%A Wenkun Huang
%A Huan Peng
%A Haibo Long
%A <br>王高峰
%A 彭德良
%A 孙建华
%A 黄文坤
%A 彭焕
%A 龙海波
%J 生物工程学报
%D 2011
%I 
%X The Cathepsin L-like cysteine proteinase genes (cpls) are multifunction genes related to the parasitic abilities of plant parasitic nematodes. A new cathepsin L-like cysteine proteinase gene (Dd-cpl-1) (GenBank Accession GQ 180107) was cloned from Ditylenchus destructor by RT-PCR and RACE. The cDNA sequence consisted of a 1 131 bp open reading frame (ORF) encoding 376 amino acid residues that were franked by a 29 bp 5'-untranslated region (UTR) and a 159 bp 3'-UTR. Genomic sequence analysis showed that Dd-cpl-1 contained 7 introns, obeyed the GT/AG rule in the splice-site junctions. Homology analysis showed that the identity was 77% between Dd-cpl-1 deduced protein Dd-CPL-1 and cathepsin L-like cysteine proteinase of Bursaphelenchus xylophilus. Multi-sequence alignment indicated that there were the catalytic triad (Cys183, His322 and Asn343) and two motifs ERFNIN motif and GNFD motif in deduced protein Dd-CPL-1. Cysteine proteinases phylogenetic analysis showed that Dd-cpl-1 belonged to the sub-clade of cathepsin L-like cysteine proteinases.
%K Ditylenchus destructor
%K cathepsin L-like cysteine proteinase
%K Dd-cpl-1<br>马铃薯腐烂茎线虫，L型半胱氨酸蛋白酶，Dd-cpl-1
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=9EFE64665428821882CF6D8E2487BC07&yid=9377ED8094509821&vid=DB817633AA4F79B9&iid=CA4FD0336C81A37A&sid=BFE7933E5EEA150D&eid=68D88C2FCF9C3098&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=25