Localization of Mitochondrial Nucleoids by Transmission Electron Microscopy Using the Transgenic Expression of the Mitochondrial Helicase Twinkle and APEX2.


Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2023
Historique:
entrez: 22 2 2023
pubmed: 23 2 2023
medline: 25 2 2023
Statut: ppublish

Résumé

Reminiscent of their evolutionary origin, mitochondria contain their own genome (mtDNA) compacted into the mitochondrial chromosome or nucleoid (mt-nucleoid). Many mitochondrial disorders are characterized by disruption of mt-nucleoids, either by direct mutation of genes involved in mtDNA organization or by interfering with other vital proteins for mitochondrial function. Thus, changes in mt-nucleoid morphology, distribution, and structure are a common feature in many human diseases and can be exploited as an indicator of cellular fitness. Electron microscopy provides the highest possible resolution that can be achieved, delivering spatial and structural information about all cellular structures. Recently, the ascorbate peroxidase APEX2 has been used to increase transmission electron microscopy (TEM) contrast by inducing diaminobenzidine (DAB) precipitation. DAB has the ability to accumulate osmium during classical EM sample preparation and, due to its high electron density, provides strong contrast for TEM. Among the nucleoid proteins, the mitochondrial helicase Twinkle fused with APEX2 has been successfully used to target mt-nucleoids, providing a tool to visualize these subcellular structures with high contrast and with the resolution of an electron microscope. In the presence of H

Identifiants

pubmed: 36807792
doi: 10.1007/978-1-0716-2922-2_13
doi:

Substances chimiques

Hydrogen Peroxide BBX060AN9V
DNA, Mitochondrial 0
DNA Helicases EC 3.6.4.-
Mitochondrial Proteins 0
APEX2 protein, human EC 4.2.99.18
Endonucleases EC 3.1.-
DNA-(Apurinic or Apyrimidinic Site) Lyase EC 4.2.99.18
Multifunctional Enzymes 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

173-188

Informations de copyright

© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

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Auteurs

David Pla-Martín (D)

Center for Physiology, Faculty of Medicine and University Hospital, University of Cologne, Cologne, Germany. dplamart@uni-koeln.de.
Center for Molecular Medicine Cologne, CMMC, University of Cologne, Cologne, Germany. dplamart@uni-koeln.de.

Felix Babatz (F)

Cologne Cluster of Excellence on Cellular stress response in Aging-associated Disease, CECAD, University of Cologne, Cologne, Germany.

Astrid C Schauss (AC)

Cologne Cluster of Excellence on Cellular stress response in Aging-associated Disease, CECAD, University of Cologne, Cologne, Germany.

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