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Full-Text Articles in Life Sciences
Ribotoxic Stress Response: Activation Of The Stress-Activated Protein Kinase Jnk1 By Inhibitors Of The Peptidyl Transferase Reaction And By Sequence-Specific Rna Damage To The Alpha-Sarcin/Ricin Loop In The 28s Rrna, Mihail S. Iordanov, David Pribnow, Jennifer L. Magun, Thanh-Hoai Dinh, Jean A. Pearson, Steven Li-Ye Chen, Bruce E. Magun
Ribotoxic Stress Response: Activation Of The Stress-Activated Protein Kinase Jnk1 By Inhibitors Of The Peptidyl Transferase Reaction And By Sequence-Specific Rna Damage To The Alpha-Sarcin/Ricin Loop In The 28s Rrna, Mihail S. Iordanov, David Pribnow, Jennifer L. Magun, Thanh-Hoai Dinh, Jean A. Pearson, Steven Li-Ye Chen, Bruce E. Magun
CUP Faculty Research
Inhibition of protein synthesis per se does not potentiate the stress-activated protein kinases (SAPKs; also known as cJun NH2-terminal kinases [JNKs]). The protein synthesis inhibitor anisomycin, however, is a potent activator of SAPKs/JNKs. The mechanism of this activation is unknown. We provide evidence that in order to activate SAPK/JNK1, anisomycin requires ribosomes that are translationally active at the time of contact with the drug, suggesting a ribosomal origin of the anisomycin-induced signaling to SAPK/JNK1. In support of this notion, we have found that aminohexose pyrimidine nucleoside antibiotics, which bind to the same region in the 28S rRNA that is the …