한빛사논문
Hanyong Jin1,6, Ji-Hyun Yeom2,3,6, Eunkyoung Shin2,4,6, Yoonjie Ha2,6, Haifeng Liu5,6, Daeyoung Kim2,6, Minju Joo2,3,6, Yong-Hak Kim4,6, Hak Kyun Kim2,6, Minkyung Ryu2,3,6, Hong-Man Kim3,6, Jeongkyu Kim2, Keun P. Kim2, Yoonsoo Hahn2, Jeehyeon Bae5 & Kangseok Lee2,3
1Key Laboratory of Natural Medicines of the Changbai Mountain, Ministry of Education, College of Pharmacy, Yanbian University, Yanji 133002 Jilin, China.
2Department of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea.
3R & D Institute, NES Biotechnology, Seoul 06974, Republic of Korea.
4Department of Microbiology, School of Medicine, Catholic University of Daegu, Daegu 42472, Republic of Korea.
5School of Pharmacy, Chung-Ang University, Seoul 06974, Republic of Korea.
6These authors contributed equally: Hanyong Jin, Ji-Hyun Yeom, Eunkyoung Shin, Yoonjie Ha, Haifeng Liu, Daeyoung Kim, Minju Joo, Yong-Hak Kim, Hak Kyun Kim, Minkyung Ryu, Hong-Man Kim.
Corresponding authors
Correspondence to Jeehyeon Bae or Kangseok Lee.
Abstract
Transfer RNA halves (tRHs) have various biological functions. However, the biogenesis of specific 5′-tRHs under certain conditions remains unknown. Here, we report that inositol-requiring enzyme 1α (IRE1α) cleaves the anticodon stem-loop region of tRNAGly(GCC) to produce 5′-tRHs (5′-tRH-GlyGCC) with highly selective target discrimination upon endoplasmic reticulum (ER) stress. Levels of 5′-tRH-GlyGCC positively affect cancer cell proliferation and modulate mRNA isoform biogenesis both in vitro and in vivo; these effects require co-expression of two nuclear ribonucleoproteins, HNRNPM and HNRNPH2, which we identify as binding proteins of 5′-tRH-GlyGCC. In addition, under ER stress in vivo, we observe simultaneous induction of IRE1α and 5′-tRH-GlyGCC expression in mouse organs and a distantly related organism, Cryptococcus neoformans. Thus, collectively, our findings indicate an evolutionarily conserved function for IRE1α-generated 5′-tRH-GlyGCC in cellular adaptation upon ER stress.
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