A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing

Guodong Xie, Tommy V. Vo, Gobi Thillainadesan, Sahana Holla, Beibei Zhang, Yiyang Jiang, Mengqi Lv, Zheng Xu, Chongyuan Wang, Vanivilasini Balachandran, Yunyu Shi, Fudong Li () and Shiv I. S. Grewal ()
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Guodong Xie: University of Science and Technology of China
Tommy V. Vo: National Cancer Institute, National Institutes of Health
Gobi Thillainadesan: National Cancer Institute, National Institutes of Health
Sahana Holla: National Cancer Institute, National Institutes of Health
Beibei Zhang: University of Science and Technology of China
Yiyang Jiang: University of Science and Technology of China
Mengqi Lv: University of Science and Technology of China
Zheng Xu: University of Science and Technology of China
Chongyuan Wang: University of Science and Technology of China
Vanivilasini Balachandran: National Cancer Institute, National Institutes of Health
Yunyu Shi: University of Science and Technology of China
Fudong Li: University of Science and Technology of China
Shiv I. S. Grewal: National Cancer Institute, National Institutes of Health

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: Abstract Gene regulatory mechanisms rely on a complex network of RNA processing factors to prevent untimely gene expression. In fission yeast, the highly conserved ortholog of human ERH, called Erh1, interacts with the YTH family RNA binding protein Mmi1 to form the Erh1-Mmi1 complex (EMC) implicated in gametogenic gene silencing. However, the structural basis of EMC assembly and its functions are poorly understood. Here, we present the co-crystal structure of the EMC that consists of Erh1 homodimers interacting with Mmi1 in a 2:2 stoichiometry via a conserved molecular interface. Structure-guided mutation of the Mmi1Trp112 residue, which is required for Erh1 binding, causes defects in facultative heterochromatin assembly and gene silencing while leaving Mmi1-mediated transcription termination intact. Indeed, EMC targets masked in mmi1∆ due to termination defects are revealed in mmi1W112A. Our study delineates EMC requirements in gene silencing and identifies an ERH interface required for interaction with an RNA binding protein.

Date: 2019
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DOI: 10.1038/s41467-018-08273-9

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