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Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex

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Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex. / Bono, Fulvia; Ebert, Judith; Unterholzner, Leonie; Güttler, Thomas; Izaurralde, Elisa; Conti, Elena.

In: EMBO Reports, Vol. 5, No. 3, 03.2004, p. 304-310.

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Bono, F, Ebert, J, Unterholzner, L, Güttler, T, Izaurralde, E & Conti, E 2004, 'Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex', EMBO Reports, vol. 5, no. 3, pp. 304-310. https://doi.org/10.1038/sj.embor.7400091

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Bono, Fulvia ; Ebert, Judith ; Unterholzner, Leonie ; Güttler, Thomas ; Izaurralde, Elisa ; Conti, Elena. / Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex. In: EMBO Reports. 2004 ; Vol. 5, No. 3. pp. 304-310.

Bibtex

@article{07733200d2944da79c8397f6e4b7c9a1,
title = "Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex",
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.",
keywords = "Amino Acid Sequence, Animals, Conserved Sequence, Crystallography, X-Ray, Cytosol, Dimerization, Drosophila Proteins, Electrophoretic Mobility Shift Assay, HeLa Cells, Humans, Immunochemistry, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, RNA Splicing, RNA Stability, RNA-Binding Proteins, Sequence Alignment",
author = "Fulvia Bono and Judith Ebert and Leonie Unterholzner and Thomas G{\"u}ttler and Elisa Izaurralde and Elena Conti",
year = "2004",
month = mar,
doi = "10.1038/sj.embor.7400091",
language = "English",
volume = "5",
pages = "304--310",
journal = "EMBO Reports",
issn = "1469-221X",
publisher = "Nature Publishing Group",
number = "3",

}

RIS

TY - JOUR

T1 - Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex

AU - Bono, Fulvia

AU - Ebert, Judith

AU - Unterholzner, Leonie

AU - Güttler, Thomas

AU - Izaurralde, Elisa

AU - Conti, Elena

PY - 2004/3

Y1 - 2004/3

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Conserved Sequence

KW - Crystallography, X-Ray

KW - Cytosol

KW - Dimerization

KW - Drosophila Proteins

KW - Electrophoretic Mobility Shift Assay

KW - HeLa Cells

KW - Humans

KW - Immunochemistry

KW - Molecular Sequence Data

KW - Nuclear Proteins

KW - Protein Binding

KW - Protein Interaction Mapping

KW - Protein Structure, Tertiary

KW - RNA Splicing

KW - RNA Stability

KW - RNA-Binding Proteins

KW - Sequence Alignment

U2 - 10.1038/sj.embor.7400091

DO - 10.1038/sj.embor.7400091

M3 - Journal article

C2 - 14968132

VL - 5

SP - 304

EP - 310

JO - EMBO Reports

JF - EMBO Reports

SN - 1469-221X

IS - 3

ER -