Article
Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2.
Genes & development - 15 May 2002
Qiu Hongfang, Hu Cuihua, Dong Jinsheng, Hinnebusch Alan G
Abstract excerpt
The protein kinase GCN2 is activated in amino acid-starved cells on binding of uncharged tRNA to a histidyl-tRNA synthetase (HisRS)-related domain. We isolated two point mutations in the protein kinase (PK) domain, R794G and F842L, that permit strong kinase activity in the absence of tRNA binding. These mutations also bypass the requirement for ribosome binding, dimerization, and association with the GCN1/GCN20...
Topics
- Binding Sites
- Dimerization
- Enzyme Activation
- Gene Expression Regulation
- Histidine-tRNA Ligase
- Mutagenesis, Site-Directed
- Mutation
- Phosphorylation
- Protein Kinases
- Protein Structure, Tertiary
- RNA, Transfer