ArticleInternational journal of molecular sciences2021
Characterization and Reconstitution of Human Lipoyl Synthase (LIAS) Supports ISCA2 and ISCU as Primary Cluster Donors and an Ordered Mechanism of Cluster Assembly.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Research advances of copper homeostasis and cuproptosis in orthopedic diseases.Cell death discovery · 2026Review
- Regulation of mitochondrial iron homeostasis in tumor cells.Molecular medicine (Cambridge, Mass.) · 2026Review
- GCSH promotes colorectal cancer progression by inhibiting Cuproptosis through the PI3K/AKT-FDX1 axis.Functional & integrative genomics · 2026Article
- NFS1 Plays a Critical Role in Regulating Ferroptosis Homeostasis.Biomolecules · 2025Review
- Spinal cord ischemia reperfusion injury induces cuproptosis in neurons.Cell & bioscience · 2025Article
- Structural basis for catalysis by human lipoyl synthase.Nature communications · 2025Article
- Characterization of tumor prognosis and sensitive chemotherapy drugs based on cuproptosis-related gene signature in ovarian cancer.BMC women's health · 2025Article
- Copper and Colorectal Cancer.Cancers · 2024Review
- Multi-omics analysis of the prognostic and biological role of cuproptosis-related gene in gastric cancer.Journal of gastrointestinal oncology · 2024Article
- Identification of cuproptosis-related genes in septic shock based on bioinformatic analysis.PloS one · 2024Article
- FDX1 regulates cellular protein lipoylation through direct binding to LIAS.bioRxiv : the preprint server for biology · 2023Article
- Cuproptosis-a potential target for the treatment of osteoporosis.Frontiers in endocrinology · 2023Review
- In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1.ACS bio & med chem Au · 2022Article
- Molecular Basis of Rare Diseases Associated to the Maturation of Mitochondrial [4Fe-4S]-Containing Proteins.Biomolecules · 2022Review
- Protein-Interaction Affinity Gradient Drives [4Fe-4S] Cluster Insertion in Human Lipoyl Synthase.Journal of the American Chemical Society · 2022Article
- Cuprotosis-related signature predicts overall survival in clear cell renal cell carcinoma.Frontiers in cell and developmental biology · 2022Article
- Bert Vallee-A 20th Century Adventure(r) in Zincology.International journal of molecular sciences · 2021Article
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5 authors.
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Abstract
Lipoyl synthase (LIAS) is an iron-sulfur cluster protein and a member of the radical S-adenosylmethionine (SAM) superfamily that catalyzes the final step of lipoic acid biosynthesis. The enzyme contains two [4Fe-4S] centers (reducing and auxiliary clusters) that promote radical formation and sulfur transfer, respectively. Most information concerning LIAS and its mechanism has been determined from prokaryotic enzymes. Herein, we detail the expression, isolation, and characterization of human LIAS, its reactivity, and evaluation of natural iron-sulfur (Fe-S) cluster reconstitution mechanisms. Cluster donation by a number of possible cluster donor proteins and heterodimeric complexes has been evaluated. [2Fe-2S]-cluster-bound forms of human ISCU and ISCA2 were found capable of reconstituting human LIAS, such that complete product turnover was enabled for LIAS, as monitored via a liquid chromatography-mass spectrometry (LC-MS) assay. Electron paramagnetic resonance (EPR) studies of native LIAS and substituted derivatives that lacked the ability to bind one or the other of LIAS's two [4Fe-4S] clusters revealed a likely order of cluster addition, with the auxiliary cluster preceding the reducing [4Fe-4S] center. These results detail the trafficking of Fe-S clusters in human cells and highlight differences with respect to bacterial LIAS analogs. Likely in vivo Fe-S cluster donors to LIAS are identified, with possible connections to human disease states, and a mechanistic ordering of [4Fe-4S] cluster reconstitution is evident.
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