Literature DB >> 20057060

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

Filipp Frank1, Geneviève Virgili, Nahum Sonenberg, Bhushan Nagar.   

Abstract

Death-associated protein 5 (DAP5) is a member of the eIF4G family of scaffolding proteins that mediate cap-independent translation initiation by recruiting the translational machinery to internal ribosomal entry sites (IRESs) on mRNA. The MIF4G domain of DAP5 directly interacts with the eukaryotic initiation factors eIF4A and eIF3 and enhances the translation of several viral and cellular IRESs. Here, the crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5 is presented.

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Year:  2009        PMID： 20057060      PMCID： PMC2805526          DOI： 10.1107/S1744309109044315

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  28 in total

1.  A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery.

Authors:  J Marcotrigiano; I B Lomakin; N Sonenberg; T V Pestova; C U Hellen; S K Burley
Journal:  Mol Cell       Date:  2001-01       Impact factor: 17.970

Review 2.  Translational control in stress and apoptosis.

Authors:  Martin Holcik; Nahum Sonenberg
Journal:  Nat Rev Mol Cell Biol       Date:  2005-04       Impact factor: 94.444

3.  Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions.

Authors:  Patrick Schütz; Mario Bumann; Anselm Erich Oberholzer; Christoph Bieniossek; Hans Trachsel; Michael Altmann; Ulrich Baumann
Journal:  Proc Natl Acad Sci U S A       Date:  2008-07-07       Impact factor: 11.205

4.  Crystallography & NMR system: A new software suite for macromolecular structure determination.

Authors:  A T Brünger; P D Adams; G M Clore; W L DeLano; P Gros; R W Grosse-Kunstleve; J S Jiang; J Kuszewski; M Nilges; N S Pannu; R J Read; L M Rice; T Simonson; G L Warren
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1998-09-01

5.  A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme.

Authors:  S Yamanaka; K S Poksay; K S Arnold; T L Innerarity
Journal:  Genes Dev       Date:  1997-02-01       Impact factor: 11.361

6.  Solvent content of protein crystals.

Authors:  B W Matthews
Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

Review 7.  Regulation of poly(A)-binding protein through PABP-interacting proteins.

Authors:  M C Derry; A Yanagiya; Y Martineau; N Sonenberg
Journal:  Cold Spring Harb Symp Quant Biol       Date:  2006

8.  Translation driven by an eIF4G core domain in vivo.

Authors:  E De Gregorio; T Preiss; M W Hentze
Journal:  EMBO J       Date:  1999-09-01       Impact factor: 11.598

9.  Translational induction of the inhibitor of apoptosis protein HIAP2 during endoplasmic reticulum stress attenuates cell death and is mediated via an inducible internal ribosome entry site element.

Authors:  Dinesh Warnakulasuriyarachchi; Sonia Cerquozzi; Herman H Cheung; Martin Holcík
Journal:  J Biol Chem       Date:  2004-02-11       Impact factor: 5.157

10.  Translational activation of uncapped mRNAs by the central part of human eIF4G is 5' end-dependent.

Authors:  E De Gregorio; T Preiss; M W Hentze
Journal:  RNA       Date:  1998-07       Impact factor: 4.942
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  3 in total

1.  Structural analysis of the DAP5 MIF4G domain and its interaction with eIF4A.

Authors:  Geneviève Virgili; Filipp Frank; Kateryna Feoktistova; Maxime Sawicki; Nahum Sonenberg; Christopher S Fraser; Bhushan Nagar
Journal:  Structure       Date:  2013-03-07       Impact factor: 5.006

2.  Cleavage of DAP5 by coxsackievirus B3 2A protease facilitates viral replication and enhances apoptosis by altering translation of IRES-containing genes.

Authors:  P J Hanson; X Ye; Y Qiu; H M Zhang; M G Hemida; F Wang; T Lim; A Gu; B Cho; H Kim; G Fung; D J Granville; D Yang
Journal:  Cell Death Differ       Date:  2015-11-20       Impact factor: 15.828

3.  A newly identified Leishmania IF4E-interacting protein, Leish4E-IP2, modulates the activity of cap-binding protein paralogs.

Authors:  Nitin Tupperwar; Shimi Meleppattu; Rohit Shrivastava; Nofar Baron; Ayelet Gilad; Gerhard Wagner; Mélissa Léger-Abraham; Michal Shapira
Journal:  Nucleic Acids Res       Date:  2020-05-07       Impact factor: 16.971
  3 in total

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