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[Cloning and sequence analysis of a new cathepsin L-like cysteine proteinase gene from Ditylenchus destructor].

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.
AuthorsGaofeng Wang, Deliang Peng, Jianhua Sun, Wenkun Huang, Huan Peng, Haibo Long
JournalSheng 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
PMID21553491 (Publication Type: English Abstract, Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Cysteine Proteases
  • Cathepsin L
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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