The tRNA-binding moiety in GCN2 contains a dimerization domain that interacts with the kinase domain and is required for tRNA binding and kinase activation

Lignende værker

• Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2
  af: Qiu, Hongfang, et al.
  Udgivet: (2002)
• Dimerization by Translation Initiation Factor 2 Kinase GCN2 Is Mediated by Interactions in the C-Terminal Ribosome-Binding Region and the Protein Kinase Domain
  af: Qiu, Hongfang, et al.
  Udgivet: (1998)
• Interaction between the tRNA-Binding and C-Terminal Domains of Yeast Gcn2 Regulates Kinase Activity In Vivo
  af: Lageix, Sebastien, et al.
  Udgivet: (2015)
• An Array of Coactivators Is Required for Optimal Recruitment of TATA Binding Protein and RNA Polymerase II by Promoter-Bound Gcn4p
  af: Qiu, Hongfang, et al.
  Udgivet: (2004)
• Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells
  af: Sattlegger, Evelyn, et al.
  Udgivet: (2000)