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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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| Glavni autori: | , , , |
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| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
Cold Spring Harbor Laboratory Press
2002
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| Teme: | |
| Online pristup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC186288/ https://ncbi.nlm.nih.gov/pubmed/12023305 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1101/gad.979402 |
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