利用酵母双杂交系统筛选TRADD的互作牛分枝杆菌蛋白

doi:10.16431/j.cnki.1671-7236.2018.11.006

Abstract

Abstract:

To investigate the mechanism of Mycobacterium bovis inhibiting apoptosis,proteins interacted with human TNFR1 associated death domain (TRADD) were screened by yeast two-hybrid system.In order to construct the genome library,the genome of Mycobacterium bovis was digested by Sau3AⅠ,and then inserted into the vector pGADT7,and transformed into E.coli DH5α.tradd gene was amplified by PCR and inserted into the vector pGBKT7.The recombinant vector named pGBKT7-tradd was transformed into yeast Y2HGold.The genome library of Mycobacterium bovis was screened to obtain positive clones interacting with human TRADD.The positive clones were confirmed by DNA sequencing and BLAST.The results showed that the titer of library was 2×10⁶ CFU with the average of inserted fragments about 1.5 kb,and the recombinant rate was >95%.TRADD expression without toxicity and autoactivation in yeast was detected by Western blotting.Seven proteins interacting with TRADD were obtained by homology analysis from 20 positive colonies.The candidate proteins in the study were provided the clue to research the infection mechanism of Mycobacterium bovis.

Key words: Mycobacterium bovis; tumor necrosis factor (TNF); TRADD; apoptosis

CLC Number:

Q812

HE Ping, ZHAO Mengcheng, WANG Ling, HUANG Zengshuai, CHEN Bao, HUANG Junfeng, SONG Houhui, YANG Yang. Screening of Mycobacterium bovis Proteins Interacting with TRADD by Yeast Two-hybrid System[J]. , 2018, 45(11): 3018-3024.

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Screening of Mycobacterium bovis Proteins Interacting with TRADD by Yeast Two-hybrid System

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