دورية أكاديمية
Iron-regulated assembly of the cytosolic iron-sulfur cluster biogenesis machinery.
| العنوان: | Iron-regulated assembly of the cytosolic iron-sulfur cluster biogenesis machinery. |
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| المؤلفون: | Fan X; Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, California, USA; Molecular Biology Institute, University of California, Los Angeles, California, USA., Barshop WD; Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, California, USA., Vashisht AA; Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, California, USA., Pandey V; Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, California, USA., Leal S; Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, California, USA., Rayatpisheh S; Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, California, USA., Jami-Alahmadi Y; Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, California, USA., Sha J; Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, California, USA., Wohlschlegel JA; Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, California, USA. Electronic address: jwohl@mednet.ucla.edu. |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 2022 Jul; Vol. 298 (7), pp. 102094. Date of Electronic Publication: 2022 May 30. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Iron*/metabolism , Iron-Sulfur Proteins*/biosynthesis , Iron-Sulfur Proteins*/metabolism, Cytosol/metabolism ; GTP-Binding Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Oxygen/metabolism ; Reactive Oxygen Species/metabolism ; Sulfur/metabolism |
| مستخلص: | The cytosolic iron-sulfur (Fe-S) cluster assembly (CIA) pathway delivers Fe-S clusters to nuclear and cytosolic Fe-S proteins involved in essential cellular functions. Although the delivery process is regulated by the availability of iron and oxygen, it remains unclear how CIA components orchestrate the cluster transfer under varying cellular environments. Here, we utilized a targeted proteomics assay for monitoring CIA factors and substrates to characterize the CIA machinery. We find that nucleotide-binding protein 1 (NUBP1/NBP35), cytosolic iron-sulfur assembly component 3 (CIAO3/NARFL), and CIA substrates associate with nucleotide-binding protein 2 (NUBP2/CFD1), a component of the CIA scaffold complex. NUBP2 also weakly associates with the CIA targeting complex (MMS19, CIAO1, and CIAO2B) indicating the possible existence of a higher order complex. Interactions between CIAO3 and the CIA scaffold complex are strengthened upon iron supplementation or low oxygen tension, while iron chelation and reactive oxygen species weaken CIAO3 interactions with CIA components. We further demonstrate that CIAO3 mutants defective in Fe-S cluster binding fail to integrate into the higher order complexes. However, these mutants exhibit stronger associations with CIA substrates under conditions in which the association with the CIA targeting complex is reduced suggesting that CIAO3 and CIA substrates may associate in complexes independently of the CIA targeting complex. Together, our data suggest that CIA components potentially form a metabolon whose assembly is regulated by environmental cues and requires Fe-S cluster incorporation in CIAO3. These findings provide additional evidence that the CIA pathway adapts to changes in cellular environment through complex reorganization. Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article. (Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.) |
| معلومات مُعتمدة: | R01 GM089778 United States GM NIGMS NIH HHS; R01 GM112763 United States GM NIGMS NIH HHS; T32 GM007185 United States GM NIGMS NIH HHS |
| فهرسة مساهمة: | Keywords: cytosolic iron–sulfur cluster assembly (CIA); iron–sulfur protein; metalloprotein; protein–protein interaction; proteomics; redox regulation |
| المشرفين على المادة: | 0 (Intracellular Signaling Peptides and Proteins) 0 (Iron-Sulfur Proteins) 0 (Reactive Oxygen Species) 70FD1KFU70 (Sulfur) E1UOL152H7 (Iron) EC 3.6.1.- (GTP-Binding Proteins) S88TT14065 (Oxygen) |
| تواريخ الأحداث: | Date Created: 20220602 Date Completed: 20220726 Latest Revision: 20220728 |
| رمز التحديث: | 20240829 |
| مُعرف محوري في PubMed: | PMC9243173 |
| DOI: | 10.1016/j.jbc.2022.102094 |
| PMID: | 35654137 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1083-351X |
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| DOI: | 10.1016/j.jbc.2022.102094 |