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Caspase‐mediated cleavage and DNase activity of the translation initiation factor 3, subunit G (eIF3g)
Author(s) -
Kim Jong-Tae,
Lee Seon-Jin,
Kim Bo-Yeon,
Lee Chul-Ho,
Yeom Young Il,
Choe Yong-Kyung,
Yoon Do-Young,
Chae Suhn-Kee,
Kim Jung Woo,
Yang Young,
Lim Jong-Seok,
Lee Hee Gu
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.09.027
Subject(s) - cleavage (geology) , caspase , protein subunit , microbiology and biotechnology , eif4g , eukaryotic translation initiation factor 4 gamma , eukaryotic translation , translation (biology) , caspase 2 , initiation factor , biology , nlrp1 , apoptosis , chemistry , biochemistry , programmed cell death , messenger rna , gene , paleontology , fracture (geology)
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 (SLRD 220 G) 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.