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Publication Abstract from PubMed

The LSM domain-containing protein LSM14/Rap55 plays a role in mRNA decapping, translational repression, and RNA granule (P-body) assembly. How LSM14 interacts with the mRNA silencing machinery, including the eIF4E-binding protein 4E-T and the DEAD-box helicase DDX6, is poorly understood. Here we report the crystal structure of the LSM domain of LSM14 bound to a highly conserved C-terminal fragment of 4E-T. The 4E-T C-terminus forms a bi-partite motif that wraps around the N-terminal LSM domain of LSM14. We also determined the crystal structure of LSM14 bound to the C-terminal RecA-like domain of DDX6. LSM14 binds DDX6 via a unique non-contiguous motif with distinct directionality as compared to other DDX6-interacting proteins. Together with mutational and proteomic studies, the LSM14-DDX6 structure reveals that LSM14 has adopted a divergent mode of binding DDX6 in order to support the formation of mRNA silencing complexes and P-body assembly.

Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes.,Brandmann T, Fakim H, Padamsi Z, Youn JY, Gingras AC, Fabian MR, Jinek M EMBO J. 2018 Mar 6. pii: embj.201797869. doi: 10.15252/embj.201797869. PMID:29510985^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.