Dithiothreitol causes toxicity in


Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
19 04 2022
Historique:
received: 01 12 2021
accepted: 17 04 2022
pubmed: 20 4 2022
medline: 14 5 2022
entrez: 19 4 2022
Statut: epublish

Résumé

The redox reagent dithiothreitol (DTT) causes stress in the endoplasmic reticulum (ER) by disrupting its oxidative protein folding environment, which results in the accumulation and misfolding of the newly synthesized proteins. DTT may potentially impact cellular physiology by ER-independent mechanisms; however, such mechanisms remain poorly characterized. Using the nematode model Animal and plant cells synthesize a significant fraction of their proteins on a structure known as the endoplasmic reticulum. Researchers often use the molecule dithiothreitol to specifically target this compartment and learn more about its role. The toxin works by disturbing the complex chemical environment present in the reticulum, which is required for the proteins to assemble properly. However, it is important to clarify whether dithiothreitol could also affect other parts of the cell, as this could give rise to misleading results. To explore this possibility, Gokul G and Jogender Singh studied the effects of dithiothreitol on the millimetre-long roundworm

Autres résumés

Type: plain-language-summary (eng)
Animal and plant cells synthesize a significant fraction of their proteins on a structure known as the endoplasmic reticulum. Researchers often use the molecule dithiothreitol to specifically target this compartment and learn more about its role. The toxin works by disturbing the complex chemical environment present in the reticulum, which is required for the proteins to assemble properly. However, it is important to clarify whether dithiothreitol could also affect other parts of the cell, as this could give rise to misleading results. To explore this possibility, Gokul G and Jogender Singh studied the effects of dithiothreitol on the millimetre-long roundworm

Identifiants

pubmed: 35438636
doi: 10.7554/eLife.76021
pii: 76021
pmc: PMC9090326
doi:
pii:

Substances chimiques

Caenorhabditis elegans Proteins 0
Homocysteine 0LVT1QZ0BA
S-Adenosylmethionine 7LP2MPO46S
Dithiothreitol T8ID5YZU6Y

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIH HHS
ID : P40 OD010440
Pays : United States

Informations de copyright

© 2022, G and Singh.

Déclaration de conflit d'intérêts

GG, JS No competing interests declared

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Auteurs

Gokul G (G)

Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, Bhopal, India.

Jogender Singh (J)

Department of Biological Sciences, Indian Institute of Science Education and Research, Mohali, Mohali, India.

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Classifications MeSH