Cloning and sequence analysis of a new cathepsin L-like cysteine proteinase gene from Ditylenchus destructor / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 60-68, 2011.
Article
in Chinese
| WPRIM
| ID: wpr-351533
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Parasitology
/
Phylogeny
/
Solanum tuberosum
/
Molecular Sequence Data
/
Sequence Alignment
/
Amino Acid Sequence
/
Cloning, Molecular
/
Sequence Homology, Amino Acid
/
Genes, Helminth
/
Sequence Analysis, Protein
Limits:
Animals
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2011
Type:
Article
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