- AutorIn
- Uta Gey
- Cornelia Czupalla
- Bernard Hoflack
- Udo Krause
- Gerhard Rödel
- Titel
- Proteomic Analysis Reveals a Novel Function of the Kinase Sat4p in Saccharomyces cerevisiae Mitochondria
- Zitierfähige Url:
- https://nbn-resolving.org/urn:nbn:de:bsz:14-qucosa-165311
- Quellenangabe
- PLoS ONE 9(8): e103956, ISSN: 1932-6203
- Erstveröffentlichung
- 2014
- Abstract (EN)
- The Saccharomyces cerevisiae kinase Sat4p has been originally identified as a protein involved in salt tolerance and stabilization of plasma membrane transporters, implicating a cytoplasmic localization. Our study revealed an additional mitochondrial (mt) localization, suggesting a dual function for Sat4p. While no mt related phenotype was observed in the absence of Sat4p, its overexpression resulted in significant changes of a specific mitochondrial subproteome. As shown by a comparative two dimensional difference gel electrophoresis (2D-DIGE) approach combined with mass spectrometry, particularly two groups of proteins were affected: the iron-sulfur containing aconitase-type proteins (Aco1p, Lys4p) and the lipoamide-containing subproteome (Lat1p, Kgd2p and Gcv3p). The lipoylation sites of all three proteins could be assigned by nanoLC-MS/MS to Lys75 (Lat1p), Lys114 (Kgd2p) and Lys102 (Gcv3p), respectively. Sat4p overexpression resulted in accumulation of the delipoylated protein variants and in reduced levels of aconitase-type proteins, accompanied by a decrease in the activities of the respective enzyme complexes. We propose a regulatory role of Sat4p in the late steps of the maturation of a specific subset of mitochondrial iron-sulfur cluster proteins, including Aco1p and lipoate synthase Lip5p. Impairment of the latter enzyme may account for the observed lipoylation defects.
- Andere Ausgabe
- DOI: 10.1371/journal.pone.0103956
- Link zur Originalpublikation in der Zeitschrift PLOS ONE.
Link: http://dx.doi.org/10.1371/journal.pone.0103956 - Freie Schlagwörter (DE)
- Mitochondrien, Proteine, Membrane,TU Dresden, Publikationsfonds
- Freie Schlagwörter (EN)
- Mitochondria, Hyperexpression techniques, Lipoylation, Membrane proteins, Technical University Dresden, Publication funds
- Klassifikation (DDC)
- 570
- Klassifikation (RVK)
- WE 3100
- Verlag
- Public Library of Science, San Francisco, USA
- URN Qucosa
- urn:nbn:de:bsz:14-qucosa-165311
- Veröffentlichungsdatum Qucosa
- 07.05.2015
- Dokumenttyp
- Artikel
- Sprache des Dokumentes
- Englisch
- Lizenz / Rechtehinweis
- CC BY 4.0