Description

• Title:
  Eukaryotic translation initiation is controlled by cooperativity effects within ternary complexes of 4E-BP1, eIF4E, and the mRNA 50 cap
• Creator:
  Modrak-Wójcik, Anna;
  Górka, Michał;
  Niedźwiecka, Katarzyna;
  Zdanowski, Konrad;
  Żuberek, Joanna;
  Niedźwiecka, Anna;
  Stolarski, Ryszard
• Description:
  Initiation is the rate-limiting step during mRNA 50 cap-dependent translation, and thus a target of a strict control in the eukaryotic cell. It is shown here by analytical ultracentrifugation and fluorescence spectroscopy that the affinity of the human translation inhibitor, eIF4E-binding protein (4E-BP1), to the translation initiation factor 4E is significantly higher when eIF4E is bound to the cap. The 4E-BP1 binding stabilizes the active eIF4E conformation and, on the other hand, can facilitate dissociation of eIF4E from the cap. These findings reveal the particular allosteric effects forming a thermodynamic cycle for the cooperative regulation of the translation initiation inhibition.
• Object availability:
  free access
• Date:
  2013.12.11
• Type:
  Article;
  PeerReviewed
• Language:
  English
• Format:
  application/msword
• Publisher:
  elsevier
• Relation: http://eprints.ibb.waw.pl/607 ;http://www.sciencedirect.com/science/article/pii/S0014579313008132 ;doi: 10.1016/j.febslet.2013.10.043.
• Subject:
  QP Physiology
• Identifier: http://eprints.ibb.waw.pl/607/13/4E-BP_2013_revised_rev_fin.docx ;
  Modrak-Wójcik, Anna and Górka, Michał and Niedźwiecka, Katarzyna and Zdanowski, Konrad and Żuberek, Joanna and Niedźwiecka, Anna and Stolarski, Ryszard (2013) Eukaryotic translation initiation is controlled by cooperativity effects within ternary complexes of 4E-BP1, eIF4E, and the mRNA 50 cap. FEBSLetters, 587 (24). pp. 3928-3934. ISSN 0014-5793
• Data provider:
  Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk
• Can I use it?:
  seek permission
• Type:
  other