Research Article

Cloning, Expression and Purification of MGG_14095 Gene of Magnaporthe grisea  

Shuang Wang1,2,3 , Yongsheng Chen2,3,4 , Fenglan Huang2,3,4 , Guorui Li2,3,4
1 College of Life Sciences and Food, Inner Mongolia University for Nationalities, Inner Mongolia Tongliao,028000,China
2 Inner Mongolia Industrial Engineering Research Center of Universities for Castor, Inner Mongolia Tongliao,028000,China
3 Inner Mongolia Key Laboratory of Castor Breeding, Inner Mongolia Tongliao,028000,China
4 Inner Mongolia Collaborative Innovation Center for Castor Industry, Inner Mongolia Tongliao,028000,China
Author    Correspondence author
Rice Genomics and Genetics, 2020, Vol. 11, No. 1   doi: 10.5376/rgg.2020.11.0001
Received: 06 May, 2020    Accepted: 07 May, 2020    Published: 05 Jun., 2020
© 2020 BioPublisher Publishing Platform
This article was first published in Genomics and Applied Biology in Chinese, and here was authorized to translate and publish the paper in English under the terms of Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:

Wang S., Li G.R., Chen Y.S., and Huang F.L., 2020, Cloning, expression and purification of MGG_14095 gene of Magnaporthe grisea, 11(1): 1-8 (doi: 10.5376/rgg.2020.11.0001)


Magnaporthe grisea is the most harmful pathogen in the world for rice and the main model organism for elucidating the molecular basis of plant fungal disease interaction. Carrying out relevant research of the growth and development of Magnaporthe grisea has a great significance for the control of Magnaporthe grisea. MGG_14095 gene is the pathogenic gene of Magnaporthe grisea. The bioinformatics prediction of MGG_14095 protein showed that the isoelectric point (PI) of MGG_14095 protein was 5.72, and the instability index was 50.99, belonging to the acid unstable protein and the α/β hydrolase superfamily, containing the keratinase conservative domain; having obvious transmembrane structure and signal peptide cutting site, belonging to the secretory protein. In this study, the MGG_14095 (38~281) gene of Magnaporthe grisea was cloned, and the prokaryotic expression system pETM20-MGG_14095 (38~28) was constructed. We use the stepwise chromatography to purify MGG_14095 protein, and the high-purity soluble target protein was obtained successfully. The results provided for the analysis of MGG_14095(38~281) protein structure, the exploration of pathogenetic mechanism of Magnaporthe grisea and the control of Magnaporthe grisea Certain theoretical and experimental basis.

Magnaporthe grisea; MGG_14095 protein; Expression and purification
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