دورية أكاديمية
Acetyl-CoA synthetase (ACSS2) does not generate butyryl- and crotonyl-CoA.
| العنوان: | Acetyl-CoA synthetase (ACSS2) does not generate butyryl- and crotonyl-CoA. |
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| المؤلفون: | Zeaiter N; Univ. Grenoble Alpes, Inserm U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA), 38058 Grenoble, France., Belot L; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 38000 Grenoble, France., Cunin V; Univ. Grenoble Alpes, CNRS, UMR 5525, VetAgro Sup, Grenoble INP, CHU Grenoble Alpes, TIMC, 38000 Grenoble, France., Nahed RA; Univ. Grenoble Alpes, Inserm U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA), 38058 Grenoble, France., Tokarska-Schlattner M; Univ. Grenoble Alpes, Inserm U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA), 38058 Grenoble, France., Le Gouellec A; Univ. Grenoble Alpes, CNRS, UMR 5525, VetAgro Sup, Grenoble INP, CHU Grenoble Alpes, TIMC, 38000 Grenoble, France., Petosa C; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 38000 Grenoble, France., Khochbin S; Univ. Grenoble Alpes, Inserm U1209 and CNRS UMR5309, Institute for Advanced Biosciences (IAB), 38058 Grenoble, France. Electronic address: saadi.khochbin@univ-grenoble-alpes.fr., Schlattner U; Univ. Grenoble Alpes, Inserm U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA), 38058 Grenoble, France; Institut Universitaire de France, Paris, France. Electronic address: uwe.schlattner@univ-grenoble-alpes.fr. |
| المصدر: | Molecular metabolism [Mol Metab] 2024 Mar; Vol. 81, pp. 101903. Date of Electronic Publication: 2024 Feb 16. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier GmbH Country of Publication: Germany NLM ID: 101605730 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2212-8778 (Electronic) Linking ISSN: 22128778 NLM ISO Abbreviation: Mol Metab Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: [München] : Elsevier GmbH, 2012- |
| مواضيع طبية MeSH: | Lysine* , Acyl Coenzyme A*/metabolism, Acetyl Coenzyme A ; Acetates ; Histones |
| مستخلص: | Acetyl and other acyl groups from different short-chain fatty acids (SCFA) competitively modify histones at various lysine sites. To fully understand the functional significance of such histone acylation, a key epigenetic mechanism, it is crucial to characterize the cellular sources of the corresponding acyl-CoA molecules required for the lysine modification. Like acetate, SCFAs such as propionate, butyrate and crotonate are thought to be the substrates used to generate the corresponding acyl-CoAs by enzymes known as acyl-CoA synthetases. The acetyl-CoA synthetase, ACSS2, which produces acetyl-CoA from acetate in the nucleocytoplasmic compartment, has been proposed to also mediate the synthesis of acyl-CoAs such as butyryl- and crotonyl-CoA from the corresponding SCFAs. This idea is now widely accepted and is sparking new research projects. However, based on our direct in vitro experiments with purified or recombinant enzymes and structural considerations, we demonstrate that ACSS2 is unable to mediate the generation of non-acetyl acyl-CoAs like butyryl- and crotonyl-CoA. It is therefore essential to re-examine published data and corresponding discussions in the light of this new finding. Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (Copyright © 2024 The Author(s). Published by Elsevier GmbH.. All rights reserved.) |
| فهرسة مساهمة: | Keywords: Acyl-CoA; Epigenetics; Histone acylation; Protein acylation; Substrate specificity |
| المشرفين على المادة: | 992-67-6 (crotonyl-coenzyme A) 72-89-9 (Acetyl Coenzyme A) K3Z4F929H6 (Lysine) 0 (Acyl Coenzyme A) 0 (Acetates) 0 (Histones) |
| تواريخ الأحداث: | Date Created: 20240218 Date Completed: 20240308 Latest Revision: 20240308 |
| رمز التحديث: | 20240308 |
| مُعرف محوري في PubMed: | PMC10906504 |
| DOI: | 10.1016/j.molmet.2024.101903 |
| PMID: | 38369012 |
| قاعدة البيانات: | MEDLINE |
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Full Text Finder | تدمد: | 2212-8778 |
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| DOI: | 10.1016/j.molmet.2024.101903 |