Functional characterization of human class I and class II mitochondrial glutaredoxins

Medientyp: E-Book; Hochschulschrift

Titel: Functional characterization of human class I and class II mitochondrial glutaredoxins

Beteiligte: Trnka, Daniel [Verfasser:in]; Helm, Christiane A. [Akademische:r Betreuer:in]; Deponte, Marcel [Akademische:r Betreuer:in]

Körperschaft: Universität Greifswald

Erschienen: Greifswald, 31. Oktober 2018

Umfang: 1 Online-Ressource (PDF-Datei: 136 Seiten, 32400 Kilobyte); Illustrationen (teilweise farbig), Diagramme (teilweise farbig)

Sprache: Englisch

Identifikator:

RVK-Notation: WD 5100 : Biologisch inaktive Proteine und Proteide insgesamt, auch: Proteinfaltung, Proteinbiosynthese

Schlagwörter: Doxorubicin > Glutaredoxin > Glutathion > Mitochondrium > Proteine > Thiole > Thioredoxine > Oxidoreductasen > Eisen-Schwefel-Proteide > Cluster > Katalytische Aktivität

Entstehung:

Hochschulschrift: Dissertation, Mathematisch-Naturwissenschaftliche Fakultät der Universität Greifswald, 2019

Anmerkungen: Literaturverzeichnis: Seite 105-123

Beschreibung: Biochemie, Doxorubicin, Glutaredoxin, Glutathion, Mitochondrium, Molekularbiologie, Proteine, Thiole, Thioredoxine, Gluglutaredoxine, Oxidoreduktase, [Fe-S] Cluster, katalytische Aktivität catalytic activity, glutaredoxins, oxidoreductase

Class I and class II glutaredoxins (Grxs) are glutathione (GSH)-dependent proteins, that function as oxidoreductases (class I) or mediate cellular iron trafficking (class II). Some members of class I Grxs like human Grx2 are able to complex a [2Fe-2S] cluster and form a dimeric holo complex, which renders them catalytically inactive and is the basis for their function as redox sensors. Class II Grxs like human Grx5 also complex [2Fe-2S] clusters, however these proteins transfer the clusters to other proteins. Both functionally distinct classes share a similar thioredoxin fold and conserved interaction sites for the non-covalently binding of GSH, which is required to complex the [2Fe-2S] cluster. Furthermore, the proteins from both classes contain a highly nucleophilic active site cysteine that would allow both classes to catalyze GSH-dependent oxidoreduction reactions. Despite of these similar features, only class I Grxs are able to form a mixed disulfide with GSH and to reversibly transfer it to protein thiols (de-/glutathionylation). Interestingly, neither class I Grxs nor class II Grxs can effectively compensate the loss of an essential member of the other class. Even though some structural differences were described earlier, the basis for their different functions remained unknown. In particular, the lack of catalytic activity of class II Grxs as oxidoreductases could not be explained. Here, we demonstrate that the different conformations of a conserved lysyl side chain ...

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