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Article: Metallo-sideromycin as a dual functional complex for combating antimicrobial resistance

TitleMetallo-sideromycin as a dual functional complex for combating antimicrobial resistance
Authors
Issue Date1-Sep-2023
PublisherNature Research
Citation
Nature Communications, 2023, v. 14, n. 1 How to Cite?
Abstract

Chromium(III) is extensively used as a supplement for muscle development and the treatment of diabetes mellitus. However, its mode of action, essentiality, and physiological/pharmacological effects have been a subject of scientific debate for over half a century owing to the failure in identifying the molecular targets of Cr(III). Herein, by integrating fluorescence imaging with a proteomic approach, we visualized the Cr(III) proteome being mainly localized in the mitochondria, and subsequently identified and validated eight Cr(III)-binding proteins, which are predominately associated with ATP synthesis. We show that Cr(III) binds to ATP synthase at its beta subunit via the catalytic residues of Thr213/Glu242 and the nucleotide in the active site. Such a binding suppresses ATP synthase activity, leading to the activation of AMPK, improving glucose metabolism, and rescuing mitochondria from hyperglycaemia-induced fragmentation. The mode of action of Cr(III) in cells also holds true in type II diabetic male mice. Through this study, we resolve the long-standing question of how Cr(III) ameliorates hyperglycaemia stress at the molecular level, opening a new horizon for further exploration of the pharmacological effects of Cr(III).


Persistent Identifierhttp://hdl.handle.net/10722/341724
ISSN
2023 Impact Factor: 14.7
2023 SCImago Journal Rankings: 4.887
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWang, Chenyuan-
dc.contributor.authorXia, Yushan-
dc.contributor.authorWang, Runming-
dc.contributor.authorLi, Jingru-
dc.contributor.authorChan, Chun-Lung-
dc.contributor.authorKao, Richard Yi-Tsun-
dc.contributor.authorToy, Patrick H-
dc.contributor.authorHo, Pak-Leung-
dc.contributor.authorLi, Hongyan-
dc.contributor.authorSun, Hongzhe-
dc.date.accessioned2024-03-20T06:58:34Z-
dc.date.available2024-03-20T06:58:34Z-
dc.date.issued2023-09-01-
dc.identifier.citationNature Communications, 2023, v. 14, n. 1-
dc.identifier.issn2041-1723-
dc.identifier.urihttp://hdl.handle.net/10722/341724-
dc.description.abstract<p>Chromium(III) is extensively used as a supplement for muscle development and the treatment of diabetes mellitus. However, its mode of action, essentiality, and physiological/pharmacological effects have been a subject of scientific debate for over half a century owing to the failure in identifying the molecular targets of Cr(III). Herein, by integrating fluorescence imaging with a proteomic approach, we visualized the Cr(III) proteome being mainly localized in the mitochondria, and subsequently identified and validated eight Cr(III)-binding proteins, which are predominately associated with ATP synthesis. We show that Cr(III) binds to ATP synthase at its beta subunit via the catalytic residues of Thr213/Glu242 and the nucleotide in the active site. Such a binding suppresses ATP synthase activity, leading to the activation of AMPK, improving glucose metabolism, and rescuing mitochondria from hyperglycaemia-induced fragmentation. The mode of action of Cr(III) in cells also holds true in type II diabetic male mice. Through this study, we resolve the long-standing question of how Cr(III) ameliorates hyperglycaemia stress at the molecular level, opening a new horizon for further exploration of the pharmacological effects of Cr(III).<br></p>-
dc.languageeng-
dc.publisherNature Research-
dc.relation.ispartofNature Communications-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleMetallo-sideromycin as a dual functional complex for combating antimicrobial resistance-
dc.typeArticle-
dc.identifier.doi10.1038/s41467-023-40828-3-
dc.identifier.scopuseid_2-s2.0-85169526246-
dc.identifier.volume14-
dc.identifier.issue1-
dc.identifier.eissn2041-1723-
dc.identifier.isiWOS:001061994900001-
dc.identifier.issnl2041-1723-

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