1hl6

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A novel mode of RBD-protein recognition in the Y14-mago complexA novel mode of RBD-protein recognition in the Y14-mago complex

Structural highlights

1hl6 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RBM8A_DROME] Involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway. Also involved in localization of osk (oskar) mRNA in the posterior pole of oocytes via its interaction with mago.[1] [2] [MGN_DROME] Participates in the bidirectional intercellular signaling between the posterior follicle cells and oocyte to establish spatial coordinates that induces axis formation. Complex with tsu is essential for cytoplasmic localization of oskar in the posterior pole of oocytes. Required for the polarization of the oocyte microtubule cytoskeleton.[3] [4] [5] [6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Y14 and Mago are conserved eukaryotic proteins that associate with spliced mRNAs in the nucleus and remain associated at exon junctions during and after nuclear export. In the cytoplasm, Y14 is involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway and, together with Mago, is involved in localization of osk (oskar) mRNA. We have determined the crystal structure of the complex between Drosophila melanogaster Y14 and Mago at a resolution of 2.5 A. The structure reveals an atypical mode of protein-protein recognition mediated by an RNA-binding domain (RBD). Instead of binding RNA, the RBD of Y14 engages its RNP1 and RNP2 motifs to bind Mago. Using structure-guided mutagenesis, we show that Mago is also a component of the NMD pathway, and that its association with Y14 is essential for function. Heterodimerization creates a single structural platform that interacts with the NMD machinery via phylogenetically conserved residues.

A novel mode of RBD-protein recognition in the Y14-Mago complex.,Fribourg S, Gatfield D, Izaurralde E, Conti E Nat Struct Biol. 2003 Jun;10(6):433-9. PMID:12730685[7]

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

References

  1. ↑ Mohr SE, Dillon ST, Boswell RE. The RNA-binding protein Tsunagi interacts with Mago Nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis. Genes Dev. 2001 Nov 1;15(21):2886-99. PMID:11691839 doi:http://dx.doi.org/10.1101/gad.927001
  2. ↑ Fribourg S, Gatfield D, Izaurralde E, Conti E. A novel mode of RBD-protein recognition in the Y14-Mago complex. Nat Struct Biol. 2003 Jun;10(6):433-9. PMID:12730685 doi:10.1038/nsb926
  3. ↑ Newmark PA, Boswell RE. The mago nashi locus encodes an essential product required for germ plasm assembly in Drosophila. Development. 1994 May;120(5):1303-13. PMID:8026338
  4. ↑ Newmark PA, Mohr SE, Gong L, Boswell RE. mago nashi mediates the posterior follicle cell-to-oocyte signal to organize axis formation in Drosophila. Development. 1997 Aug;124(16):3197-207. PMID:9272960
  5. ↑ Micklem DR, Dasgupta R, Elliott H, Gergely F, Davidson C, Brand A, Gonzalez-Reyes A, St Johnston D. The mago nashi gene is required for the polarisation of the oocyte and the formation of perpendicular axes in Drosophila. Curr Biol. 1997 Jul 1;7(7):468-78. PMID:9210377
  6. ↑ Fribourg S, Gatfield D, Izaurralde E, Conti E. A novel mode of RBD-protein recognition in the Y14-Mago complex. Nat Struct Biol. 2003 Jun;10(6):433-9. PMID:12730685 doi:10.1038/nsb926
  7. ↑ Fribourg S, Gatfield D, Izaurralde E, Conti E. A novel mode of RBD-protein recognition in the Y14-Mago complex. Nat Struct Biol. 2003 Jun;10(6):433-9. PMID:12730685 doi:10.1038/nsb926

1hl6, resolution 2.50Å

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