Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2

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. T...

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Veröffentlicht in:	Genes Dev
Hauptverfasser:	Qiu, Hongfang, Hu, Cuihua, Dong, Jinsheng, Hinnebusch, Alan G.
Format:	Artigo
Sprache:	Inglês
Veröffentlicht:	Cold Spring Harbor Laboratory Press 2002
Schlagworte:	Research Paper
Online-Zugang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC186288/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12023305/ https://ncbi.nlm.nih.govhttps://doi.org/10.1101/gad.979402
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