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Brandmann_LSM14

ABSTRACT: This set of submissions contains the mass spectrometry files for the manuscript by Tobias Brandmann et al. that describes structure function study of LSM14. Affinity-purification experiments were performed using HeLa cells expressing LSM14A wild-type and mutant constructs, and MS files were acquired on Orbitrap Elite.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Anne-Claude Gingras

PROVIDER: MSV000081830 | MassIVE | Tue Dec 19 13:29:00 GMT 2017

SECONDARY ACCESSION(S): PXD008505

REPOSITORIES: MassIVE

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Publications

Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes.

Brandmann Tobias T Fakim Hana H Padamsi Zoya Z Youn Ji-Young JY Gingras Anne-Claude AC Fabian Marc R MR Jinek Martin M

The EMBO journal 20180306 7

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 o ...[more]

PMID: 29510985

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