6AKJ

The crystal structure of EMC complex

Summary for 6AKJ

• Entry DOI: 10.2210/pdb6akj/pdb
• Descriptor: Enhancer of rudimentary homolog,YTH domain-containing protein mmi1 fusion protein, SULFATE ION (3 entities in total)
• Functional Keywords: protein-protein interaction, rna binding protein
• Biological source: Schizosaccharomyces pombe 972h- (Fission yeast); More
• Total number of polymer chains: 2
• Total formula weight: 36329.89

Authors

Li, F. (deposition date: 2018-09-01, release date: 2019-02-13, Last modification date: 2023-11-22)

Primary citation

Xie, G.,Vo, T.V.,Thillainadesan, G.,Holla, S.,Zhang, B.,Jiang, Y.,Lv, M.,Xu, Z.,Wang, C.,Balachandran, V.,Shi, Y.,Li, F.,Grewal, S.I.S.
A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing.
Nat Commun, 10:251-251, 2019

PubMed 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 Mmi1 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 mmi1. Our study delineates EMC requirements in gene silencing and identifies an ERH interface required for interaction with an RNA binding protein.

PubMed: 30651569
DOI: 10.1038/s41467-018-08273-9

Experimental method

X-RAY DIFFRACTION (2.7 Å)