Web of Science: 7 citas, Scopus: 7 citas, Google Scholar: citas,
Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3
Abrie, J. Albert (Stellenbosch University. Department of Biochemistry)
Molero Merinero, Cristina (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Strauss, Erick (Stellenbosch University. Department of Biochemistry)
Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí"

Fecha: 2015
Resumen: Saccharomyces cerevisiae Hal3 and Vhs3 are moonlighting proteins, acting both as inhibitors of the serine/threonine protein phosphatase Ppz1 and as subunits (together with Cab3) of the unique heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme of Hemiascomycetous yeast. Both these roles are essential: PPCDC catalyses the third step of coenzyme A biosynthesis, while Ppz1 inhibition is required for regulation of monovalent cation homeostasis. However, the mechanisms by which these proteins € disparate activities are regulated are not well understood. The PPCDC domains (PDs) of Hal3, Vhs3 and Cab3 constitute the minimum requirement for these proteins to show both PPCDC activity and, in the case of Hal3 and Vhs3, to bind to Ppz1. Using these PD proteins as a model system to study the possibility of dynamic interchange between these roles, we provide evidence that Hal3 binds Ppz1 as a monomer (1:1 stoichiometry), requiring it to de-oligomerize from its usual homo- and heterotrimeric states (the latter having PPCDC activity). This de-oligomerization is made possible by structural features that set Hal3 apart from Vhs3, increasing its ability to undergo monomer exchange. These findings suggest that oligomer interchange may be a significant factor in the functional regulation of these proteins and their various unrelated (moonlighting) functions.
Nota: Número d'acord de subvenció MINECO/BFU2011-30197-C03-01
Nota: Número d'acord de subvenció MINECO/BFU2014-54591-C2-1-P
Nota: Número d'acord de subvenció AGAUR/2014/SGR-4
Derechos: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. Creative Commons
Lengua: Anglès.
Documento: article ; recerca ; publishedVersion
Materia: Biocatalysis ; Cell Cycle Proteins ; Circular Dichroism ; Coenzyme A ; Flavins ; Phosphoprotein Phosphatases ; Protein Binding ; Protein Multimerization ; Protein Stability ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins ; Substrate Specificity
Publicado en: Scientific Reports, Vol. 5 (October 2015) , art. 15774, ISSN 2045-2322

DOI: 10.1038/srep15774
PMID: 26514574


17 p, 1.6 MB

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 Registro creado el 2019-04-12, última modificación el 2019-07-16



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