Supplements - The rice blast fungus MoRgs1 functioning in cAMP signaling and pathogenicity is regulated by casein kinase MoCk2 phosphorylation and modulated by membrane protein MoEmc2
Document Type
Dataset
Publication Date
2021
Publication Title
Figshare
Abstract
(A) Structure and domain prediction of MoEmc2 using SMART (http://smart.embl-heidelberg.de/). The positions of the domains within the proteins were indicated by amino acid numbers. The full length of MoEMC2 was divided into NTD, TPR, and CTD domains before being ligated in pGBKT7. (B) MoRgs1 has two DEP domains at the N-terminus and one RGS domain at the C-terminus [22, 31]. Similar methods were used to conduct the following MoRgs1 vectors in pGADT7: AD-MoRgs1, AD-N-Rgs1, and AD-C-Rgs1. (C) The full length and regions of MoRgs1 and MoEmc2 were assayed by Y2H. The yeast co-transformants expressing the bait and prey constructs were isolated on the SD-Leu-Trp plate for 3 d and screened by SD-Ade-His-Leu-Trp plates for 5 d.
DOI
10.1371/journal.ppat.1009657.s008
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This work is licensed under a Creative Commons Attribution 4.0 International License.
Recommended Citation
Yu, Rui; Shen, Xuetong; Liu, Muxing; Liu, Xinyu; Yin, Ziyi; Li, Xiao; Feng, Wanzhen; Hu, Jiexiong; Zhang, Haifeng; Zheng, Xiaobo; Wang, Ping; and Zhang, Zhengguang, "Supplements - The rice blast fungus MoRgs1 functioning in cAMP signaling and pathogenicity is regulated by casein kinase MoCk2 phosphorylation and modulated by membrane protein MoEmc2" (2021). Data Sets. 93.
https://digitalscholar.lsuhsc.edu/datasets/93
10.1371/journal.ppat.1009657.s008
Comments
Original Article: https://doi.org/10.1371/journal.ppat.1009657