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Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria.
Rocha, Agostinho G; Knight, Simon A B; Pandey, Alok; Yoon, Heeyong; Pain, Jayashree; Pain, Debkumar; Dancis, Andrew.
Afiliación
  • Rocha AG; Department of Medicine, Division of Hematology-Oncology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States.
  • Knight SAB; Department of Medicine, Division of Hematology-Oncology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States.
  • Pandey A; Department of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers University, Newark, NJ, United States.
  • Yoon H; Department of Medicine, Division of Hematology-Oncology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States.
  • Pain J; Department of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers University, Newark, NJ, United States.
  • Pain D; Department of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers University, Newark, NJ, United States.
  • Dancis A; Department of Medicine, Division of Hematology-Oncology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States. Electronic address: adancis@mail.med.upenn.edu.
Mitochondrion ; 40: 29-41, 2018 05.
Article en En | MEDLINE | ID: mdl-28941588
The cysteine desulfurase Nfs1/Isd11 uses the amino acid cysteine as the substrate and its activity is absolutely required for contributing persulfide sulfur to the essential process of iron-sulfur (Fe-S) cluster assembly in mitochondria. Here we describe a novel regulatory process involving phosphorylation of Nfs1 in mitochondria. Phosphorylation enhanced cysteine desulfurase activity, while dephosphorylation decreased its activity. Nfs1 phosphopeptides were identified, and the corresponding phosphosite mutants showed impaired persulfide formation. Nfs1 pull down from mitochondria recovered an associated kinase activity, and Yck2, a kinase present in the pull down, was able to phosphorylate Nfs1 in vitro and stimulate cysteine desulfurase activity. Yck2 exhibited an eclipsed distribution in the mitochondrial matrix, although other cellular localizations have been previously described. Mitochondria lacking the Yck2 protein kinase (∆yck2) showed less phosphorylating activity for Nfs1. Compared with wild-type mitochondria, ∆yck2 mitochondria revealed slower persulfide formation on Nfs1 consistent with a role of Yck2 in regulating mitochondrial cysteine desulfurase activity. We propose that Nfs1 phosphorylation may provide a means of rapid adaptation to increased metabolic demand for sulfur and Fe-S clusters within mitochondria.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Sulfurtransferasas / Regulación Fúngica de la Expresión Génica / Procesamiento Proteico-Postraduccional / Proteínas de Saccharomyces cerevisiae / Proteínas Mitocondriales / Quinasa de la Caseína I / Mitocondrias Idioma: En Revista: Mitochondrion Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Sulfurtransferasas / Regulación Fúngica de la Expresión Génica / Procesamiento Proteico-Postraduccional / Proteínas de Saccharomyces cerevisiae / Proteínas Mitocondriales / Quinasa de la Caseína I / Mitocondrias Idioma: En Revista: Mitochondrion Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos