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http://dx.doi.org/10.4014/jmb.2104.04021

Mitochondrial Targeting Domain Homologs Induce Necrotic Cell Death Via Mitochondrial and Endoplasmic Reticulum Disruption  

Park, Junghee (Department of Biochemistry and Molecular Biology, Chosun University School of Medicine)
Han, Ji-Hye (Department of Biochemistry and Molecular Biology, Chosun University School of Medicine)
Myung, Seung-Hyun (Department of Biochemistry and Molecular Biology, Chosun University School of Medicine)
Chung, Hea-jong (Gwangju Center, Korea Basic Science Institute)
Park, Jae-il (Gwangju Center, Korea Basic Science Institute)
Cho, Ju-Yeon (Department of Medicine, Chosun University Hospital)
Kim, Tae-Hyoung (Department of Biochemistry and Molecular Biology, Chosun University School of Medicine)
Publication Information
Journal of Microbiology and Biotechnology / v.31, no.6, 2021 , pp. 875-881 More about this Journal
Abstract
The mitochondrial targeting domain (MTD) of Noxa contributes to its mitochondrial localization and to apoptosis induction. As a peptide, MTD fused with octa-arginine (R8), a CPP, induces necrosis related to intracellular calcium influx and destruction of mitochondria and endoplasmic reticulum. We searched for homologs of MTD, and compared their cell killing capability when fused with R8. Three of the seven peptides triggered cell death with similar mechanisms. The comparative analysis of peptide sequences showed that four amino acid sites of MTD are critical in regulating necrosis, suggesting the potential to generate artificial, adjustable cytotoxic peptides, which could be effective medicines for many diseases. Thus, homologs functionality could hint to the functions of their belonging proteins.
Keywords
MTD; MTD homologs; necrotic cell death; mitochondria;
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