Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2.

Podobne zapisy

• eIF2B promotes eIF5 dissociation from eIF2•GDP to facilitate guanine nucleotide exchange for translation initiation
  od: Jennings, Martin D., i wsp.
  Wydane: (2013)
• Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2.
  od: Pavitt, G D, i wsp.
  Wydane: (1997)
• Tight Binding of the Phosphorylated α Subunit of Initiation Factor 2 (eIF2α) to the Regulatory Subunits of Guanine Nucleotide Exchange Factor eIF2B Is Required for Inhibition of Translation Initiation
  od: Krishnamoorthy, Thanuja, i wsp.
  Wydane: (2001)
• eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine–nucleotide exchange
  od: Pavitt, Graham D., i wsp.
  Wydane: (1998)
• Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo
  od: Olsen, DeAnne S., i wsp.
  Wydane: (2003)