Biotechnology Bulletin ›› 2015, Vol. 31 ›› Issue (10): 131-139.doi: 10.13560/j.cnki.biotech.bull.1985.2015.10.022

• Research report • Previous Articles     Next Articles

Cloning and Prokaryotic Expression of Dd-Gpx from Ditylenchus destructor

Liu Yang, He Xufeng, Liu Jianxi, Ding Zhong   

  1. Key Laboratory for Biology and Control of Plant Diseases and Insect Pests, College of Plant Protection, Hunan Agricultural University, Changsha 410128
  • Received:2015-01-15 Online:2015-10-28 Published:2015-10-28

Abstract: To further understand the structure and function of glutathione peroxidase, a glutathione peroxidase gene was cloned from plant-parasitic nematode(Ditylenchus destructor)using RACE method, and the gene(DdGpx)was transferred into vector of pET-41b to have the fusion expression. The full-length cDNA of DdGpx was 950 bp containing an open reading frame of 681 bp and encoding 226 amino acids. Bioinformatics analysis indicated that the N terminal of the protein had obvious signal peptide, belonging to the secretory protein. The prokaryotic expression vector pET-41b-DdGpx was constructed and then transformed into BL21(DE3), there was a apparent band in 60 kD. Mass spectrum analysis indicated that there were 7 peptides matched with D. destructor GPX protein, implying that the recombinant protein of Dd-GPX was successfully expressed

Key words: Ditylenchus destructor, glutathione peroxidase, gene cloning, prokaryotic expression