Molecular cloning and characterization of an acetylcholinesterase gene Dd-ace-2 from sweet potato stem nematode Ditylenchus destructor.
- Author:
Zhong DING
1
;
Deliang PENG
;
Wenkun HUANG
;
Wenting HE
;
Bida GAO
Author Information
1. State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100094, China.
- Publication Type:Journal Article
- MeSH:
Acetylcholinesterase;
genetics;
Amino Acid Sequence;
Animals;
Cloning, Molecular;
DNA, Complementary;
genetics;
Genes, Helminth;
genetics;
Ipomoea batatas;
parasitology;
Molecular Sequence Data;
Nematoda;
enzymology;
genetics;
Plant Stems;
parasitology;
Reverse Transcriptase Polymerase Chain Reaction;
Sequence Analysis, Protein
- From:
Chinese Journal of Biotechnology
2008;24(2):239-244
- CountryChina
- Language:Chinese
-
Abstract:
A cDNA, named Dd-ace-2, encoding an acetylcholinesterase (AChE, EC3.1.1.7), was isolated from sweet-potato-stem nematode, Ditylenchus destructor. The nucleotide and amino acid sequences among different nematode species were compared and analyzed with DNAMAN5.0, MEGA3.0 softwares. The results showed that the complete nucleotide sequence of Dd-ace-2 gene of Ditylenchus destructor contains 2425 base pairs from which deduced 734 amino acids (GenBank accession No. EF583058). The homology rates of amino acid sequences of Dd-ace-2 gene between Ditylenchus destructor and Meloidogyne incognita, Caenorhabditis elegans, Dictyocaulus viviparous were 48.0%, 42.7%, 42.1% respectively. The mature acetylcholinesterase sequences of Ditylenchus destructor may encode by the first 701 residues of deduced 734 amino acids.The conserved motifs involved in the catalytic triad, the choline binding site and 10 aromatic residues lining the catalytic gorge were present in the Dd-ace-2 deduced protein. Phylogenetic analysis based on AChEs of other nematodes and species showed that the deduced AChE formed the same cluster with ACE-2s.
