• Title/Summary/Keyword: Mitochondrial genome editing

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Mitochondrial genome editing: strategies, challenges, and applications

  • Kayeong Lim
    • BMB Reports
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    • v.57 no.1
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    • pp.19-29
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    • 2024
  • Mitochondrial DNA (mtDNA), a multicopy genome found in mitochondria, is crucial for oxidative phosphorylation. Mutations in mtDNA can lead to severe mitochondrial dysfunction in tissues and organs with high energy demand. MtDNA mutations are closely associated with mitochondrial and age-related disease. To better understand the functional role of mtDNA and work toward developing therapeutics, it is essential to advance technology that is capable of manipulating the mitochondrial genome. This review discusses ongoing efforts in mitochondrial genome editing with mtDNA nucleases and base editors, including the tools, delivery strategies, and applications. Future advances in mitochondrial genome editing to address challenges regarding their efficiency and specificity can achieve the promise of therapeutic genome editing.

DNA Barcoding for the Hydrothermal Vent Crab Austinograea Species (Crustacea: Bythograeidae) from the North Fiji Basin, Southwestern Pacific Ocean

  • Lee, Won-Kyung;Ju, Se-Jong;Hou, Bo Kyeng;Kim, Se-Joo
    • Animal Systematics, Evolution and Diversity
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    • v.35 no.1
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    • pp.30-32
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    • 2019
  • The brachyuran crab Bythograeidae Williams, 1980 is common in hydrothermal vent fields worldwide and has recorded to sixteen species of six genera. In this study, we firstly determined the cytochrome c oxidase subunit 1 (CO1) DNA barcodes for the fifth species of Austinograea, A. hourdezi, from hydrothermal vent regions of the North Fiji Basin in southwestern Pacific Ocean. All CO1 DNA barcodes of A. hourdezi were identical. The interspecies variations of three bythograeid genera were 10.9-13.3% for Austinograea, 6.6-15.7% for Bythograea, and 9.7% for Gandalfus. These results would be helpful to understand taxonomy of brachyuran crabs living in hydrothermal vent fields using CO1 DNA barcodes.

DNA Barcoding of Isaacsicalanus paucisetus (Copepoda: Calanoida: Spinocalanidae) from the Hydrothermal Vent in the North Fiji Basin, Southwestern Pacific Ocean

  • Park, Chailinn;Lee, Won-Kyung;Kim, Se-Joo;Ju, Se-Jong
    • Animal Systematics, Evolution and Diversity
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    • v.36 no.2
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    • pp.182-184
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    • 2020
  • Isaacsicalanus paucisetus Fleminger, 1983, a monotypic species of the family Spinocalanidae Vervoort, 1951, was first reported from a hydrothermal vent field in the East Pacific Rise off the mouth of the Gulf of California. The mitochondrial cytochrome oxidase I(mtCOI) DNA barcodes are considered a useful tool to assist traditional taxonomy and species discrimination in calanoid copepods. However, the mtCOI DNA barcodes of I. paucisetus have not been reported due to the species rarity and the difficulty of sampling. In this study, we firstly determined the mtCOI DNA barcodes of the I. paucisetus newly collected from a hydrothermal vent in the North Fiji Basin of the southwestern Pacific. All mtCOI DNA barcodes of I. paucisetus were identical and intraspecies variations of spinocalanid species were 0.0-3.0%. Interspecies and intergeneric variations were 13.4-25.2% and 16.7-24.1%, respectively. The DNA barcodes of I. paucisetus obtained in the present study would be helpful for understanding taxonomic relationships of widespread spinocalanid species.

Structural resemblance of the DNAJA-family protein, Tid1, to the DNAJB-family Hsp40

  • Jang, Jinhwa;Lee, Sung-Hee;Kang, Dong-Hoon;Sim, Dae-Won;Ryu, Kyung-Suk;Jo, Ku-Sung;Lee, Jinhyuk;Ryu, Hyojung;Kim, Eun-Hee;Won, Hyung-Sik;Kim, Ji-Hun
    • BMB Reports
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    • v.55 no.10
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    • pp.488-493
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    • 2022
  • The specific pair of heat shock protein 70 (Hsp70) and Hsp40 constitutes an essential molecular chaperone system involved in numerous cellular processes, including the proper folding/refolding and transport of proteins. Hsp40 family members are characterized by the presence of a conserved J-domain (JD) that functions as a co-chaperone of Hsp70. Tumorous imaginal disc 1 (Tid1) is a tumor suppressor protein belonging to the DNAJA3 subfamily of Hsp40 and functions as a co-chaperone of the mitochondrial Hsp70, mortalin. In this work, we performed nuclear magnetic resonance spectroscopy to determine the solution structure of JD and its interaction with the glycine/phenylalanine-rich region (GF-motif) of human Tid1. Notably, Tid1-JD, whose conformation was consistent with that of the DNAJB1 JD, appeared to stably interact with its subsequent GF-motif region. Collectively with our sequence analysis, the present results demonstrate that the functional and regulatory mode of Tid1 resembles that of the DNAJB1 subfamily members rather than DNAJA1 or DNAJA2 subfamily proteins. Therefore, it is suggested that an allosteric interaction between mortalin and Tid1 is involved in the mitochondrial Hsp70/Hsp40 chaperone system.