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Structure of the Y14-Magoh core of the exon junction complex.
Curr Biol. 2003 May 27; 13(11):933-41.CB

Abstract

BACKGROUND

Splicing of pre-mRNA in eukaryotes imprints the resulting mRNA with a specific multiprotein complex, the exon-exon junction complex (EJC), at the sites of intron removal. The proteins of the EJC, Y14, Magoh, Aly/REF, RNPS1, Srm160, and Upf3, play critical roles in postsplicing processing, including nuclear export and cytoplasmic localization of the mRNA, and the nonsense-mediated mRNA decay (NMD) surveillance process. Y14 and Magoh are of particular interest because they remain associated with the mRNA in the same position after its export to the cytoplasm and require translation of the mRNA for removal. This tenacious, persistent, splicing-dependent, yet RNA sequence-independent, association suggests an important signaling function and must require distinct structural features for these proteins.

RESULTS

We describe the high-resolution structure and biochemical properties of the highly conserved human Y14 and Magoh proteins. Magoh has an unusual structure comprised of an extremely flat, six-stranded anti-parallel beta sheet packed against two helices. Surprisingly, Magoh binds with high affinity to the RNP motif RNA binding domain (RBD) of Y14 and completely masks its RNA binding surface.

CONCLUSIONS

The structure and properties of the Y14-Magoh complex suggest how the pre-mRNA splicing machinery might control the formation of a stable EJC-mRNA complex at splice junctions.

Authors+Show Affiliations

Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

12781131

Citation

Lau, Chi-Kong, et al. "Structure of the Y14-Magoh Core of the Exon Junction Complex." Current Biology : CB, vol. 13, no. 11, 2003, pp. 933-41.
Lau CK, Diem MD, Dreyfuss G, et al. Structure of the Y14-Magoh core of the exon junction complex. Curr Biol. 2003;13(11):933-41.
Lau, C. K., Diem, M. D., Dreyfuss, G., & Van Duyne, G. D. (2003). Structure of the Y14-Magoh core of the exon junction complex. Current Biology : CB, 13(11), 933-41.
Lau CK, et al. Structure of the Y14-Magoh Core of the Exon Junction Complex. Curr Biol. 2003 May 27;13(11):933-41. PubMed PMID: 12781131.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure of the Y14-Magoh core of the exon junction complex. AU - Lau,Chi-Kong, AU - Diem,Michael D, AU - Dreyfuss,Gideon, AU - Van Duyne,Gregory D, PY - 2003/6/5/pubmed PY - 2004/3/6/medline PY - 2003/6/5/entrez SP - 933 EP - 41 JF - Current biology : CB JO - Curr. Biol. VL - 13 IS - 11 N2 - BACKGROUND: Splicing of pre-mRNA in eukaryotes imprints the resulting mRNA with a specific multiprotein complex, the exon-exon junction complex (EJC), at the sites of intron removal. The proteins of the EJC, Y14, Magoh, Aly/REF, RNPS1, Srm160, and Upf3, play critical roles in postsplicing processing, including nuclear export and cytoplasmic localization of the mRNA, and the nonsense-mediated mRNA decay (NMD) surveillance process. Y14 and Magoh are of particular interest because they remain associated with the mRNA in the same position after its export to the cytoplasm and require translation of the mRNA for removal. This tenacious, persistent, splicing-dependent, yet RNA sequence-independent, association suggests an important signaling function and must require distinct structural features for these proteins. RESULTS: We describe the high-resolution structure and biochemical properties of the highly conserved human Y14 and Magoh proteins. Magoh has an unusual structure comprised of an extremely flat, six-stranded anti-parallel beta sheet packed against two helices. Surprisingly, Magoh binds with high affinity to the RNP motif RNA binding domain (RBD) of Y14 and completely masks its RNA binding surface. CONCLUSIONS: The structure and properties of the Y14-Magoh complex suggest how the pre-mRNA splicing machinery might control the formation of a stable EJC-mRNA complex at splice junctions. SN - 0960-9822 UR - https://www.unboundmedicine.com/medline/citation/12781131/Structure_of_the_Y14_Magoh_core_of_the_exon_junction_complex_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0960-9822(03)00328-2 DB - PRIME DP - Unbound Medicine ER -