Caspase-mediated cleavage and DNase activity of the translation initiation factor 3, subunit G (eIF3g) |
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| Authors: | Jong-Tae Kim Seon-Jin Lee Bo-Yeon Kim Chul-Ho Lee Young Il Yeom Yong-Kyung Choe Do-Young Yoon Suhn-Kee Chae Jung Woo Kim Young Yang Jong-Seok Lim Hee Gu Lee |
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| Affiliation: | 1. Medical Genomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea;2. Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea;3. Animal Model Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea;4. Animal Department of Bioscience and Biotechnology, Konkuk University, Seoul, Republic of Korea;5. Division of Life Science, PaiChai University, Daejeon, Republic of Korea;6. Department of Biological Sciences, and the Research Center for Women’s Diseases, Sookmyung Women’s University, Seoul, Republic of Korea |
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| Abstract: | Eukaryotic translation initiation factor 3 is composed of 13 subunits (eIF3a through eIF3m) and plays an essential role in translation. During apoptosis, several caspases rapidly down-regulate protein synthesis by cleaving eIF4G, -4B, -3j, and -2α. In this study, we found that the activation of caspases by cisplatin in T24 cells induces the cleavage of subunit G of the eIF3 complex (eIF3g). The cleavage site (SLRD220G) was identified, and we found that the cleaved N-terminus was translocated to the nucleus, activating caspase-3, and that it also showed a strong DNase activity. These data demonstrate the important roles of eIF3g in the translation initiation machinery and in DNA degradation during apoptosis. |
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| Keywords: | Translation initiation factor eIF3g Caspase DNase Apoptosis |
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