Abstract |
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.
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Authors | Gaofeng Wang, Deliang Peng, Jianhua Sun, Wenkun Huang, Huan Peng, Haibo Long |
Journal | Sheng wu gong cheng xue bao = Chinese journal of biotechnology
(Sheng Wu Gong Cheng Xue Bao)
Vol. 27
Issue 1
Pg. 60-8
(Jan 2011)
ISSN: 1000-3061 [Print] China |
PMID | 21553491
(Publication Type: English Abstract, Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Cysteine Proteases
- Cathepsin L
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Topics |
- Amino Acid Sequence
- Animals
- Cathepsin L
(genetics)
- Cloning, Molecular
- Cysteine Proteases
(genetics)
- Genes, Helminth
(genetics)
- Molecular Sequence Data
- Nematoda
(enzymology, genetics)
- Phylogeny
- Sequence Alignment
- Sequence Analysis, Protein
- Sequence Homology, Amino Acid
- Solanum tuberosum
(parasitology)
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