AI Article Synopsis
- - The study focuses on the Erh1-Mmi1 complex (EMC) in fission yeast, which plays a crucial role in repressing specific gene expressions to ensure proper development.
- - Researchers provided the first detailed co-crystal structure of the EMC, revealing how Erh1 homodimers bind to Mmi1, highlighting a critical interaction for gene silencing.
- - Mutations in the Mmi1 protein that disrupt its binding to Erh1 lead to issues in gene silencing and heterochromatin assembly, while not affecting transcription termination, helping to clarify EMC's functions in regulating gene expression.
Article 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.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6335422 | PMC |
| http://dx.doi.org/10.1038/s41467-018-08273-9 | DOI Listing |
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