Cloning and sequence analysis of a new cathepsin L-like cysteine proteinase gene from Ditylenchus destructor.
- Author:
Gaofeng WANG
1
;
Deliang PENG
;
Jianhua SUN
;
Wenkun HUANG
;
Huan PENG
;
Haibo LONG
Author Information
1. College of Life Sciences, Tianjin Normal University, Tianjin 300387, China.
- Publication Type:Journal Article
- MeSH:
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
- From:
Chinese Journal of Biotechnology
2011;27(1):60-68
- CountryChina
- Language:Chinese
-
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.
