1RK8

Structure of the cytosolic protein PYM bound to the Mago-Y14 core of the exon junction complex

Summary for 1RK8

• Entry DOI: 10.2210/pdb1rk8/pdb
• Related: 1HL6 1P27 1oo0
• Descriptor: CG8781-PA protein, Mago nashi protein, Within the bgcn gene intron protein, ... (5 entities in total)
• Functional Keywords: mrna processing; rrm; rbd; nmd; oskar mrna localization, translation
• Biological source: Drosophila melanogaster (fruit fly); More
• Cellular location: Nucleus: Q9V535 P49028; Cytoplasm: P82804
• Total number of polymer chains: 3
• Total formula weight: 43107.66

Authors

Bono, F.,Ebert, J.,Guettler, T.,Izaurralde, E.,Conti, E. (deposition date: 2003-11-21, release date: 2004-04-13, Last modification date: 2024-02-14)

Primary citation

Bono, F.,Ebert, J.,Unterholzner, L.,Guettler, T.,Izaurralde, E.,Conti, E.
Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex
EMBO Rep., 5:304-310, 2004

PubMed Abstract: The exon junction complex (EJC) is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. The Mago-Y14 heterodimer is a core component of the EJC. Recently, the protein PYM has been identified as an interacting partner of Mago-Y14. Here we show that PYM is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. PYM interacts directly with Mago-Y14 by means of its N-terminal domain. The crystal structure of the Drosophila ternary complex at 1.9 A resolution reveals that PYM binds Mago and Y14 simultaneously, capping their heterodimerization interface at conserved surface residues. Formation of this ternary complex is also observed with the human proteins. Mago residues involved in the interaction with PYM have been implicated in nonsense-mediated mRNA decay (NMD). Consistently, human PYM is active in NMD tethering assays. Together, these data suggest a role for PYM in NMD.

PubMed: 14968132
DOI: 10.1038/sj.embor.7400091

Experimental method

X-RAY DIFFRACTION (1.9 Å)