Web of Science: 31 cites, Scopus: 31 cites, Google Scholar: cites,
Moonlighting Proteins Hal3 and Vhs3 Form a Heteromeric PPCDC with Ykl088w in Yeast CoA Biosynthesis
Ruiz, Amparo (Universitat Autonòma de Barcelona. Departament de Bioquimica i Biologia Molecular)
González Seviné, Asier (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Muñoz, Ivan (Universitat Autonòma de Barcelona. Departament de Bioquimica i Biologia Molecular)
Serrano, Raquel (Universitat Autonòma de Barcelona. Departament de Bioquimica i Biologia Molecular)
Abrie, J. Albert (Stellenbosch University (South Africa). Department of Biochemistry)
Strauss, Erick (Stellenbosch University (South Africa). Department of Biochemistry)
Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)

Data: 2009
Resum: Unlike most other organisms, the essential five-step Coenzyme A biosynthetic pathway has not been fully resolved in yeast. Specifically, the gene(s) encoding the phosphopantothenoylcysteine decarboxylase (PPCDC) activity still remains unidentified. Sequence homology analyses suggest three candidates, namely Ykl088w, Hal3 and Vhs3, as putative PPCDC enzymes in Saccharomyces cerevisiae. Interestingly, Hal3 and Vhs3 have been characterized as negative regulatory subunits of the Ppz1 protein phosphatase. Here we show that YKL088w does not encode a third Ppz1 regulatory subunit, and that the essential roles of Ykl088w and the Hal3/Vhs3 pair are complementary, cannot be interchanged and can be attributed to PPCDC-related functions. We demonstrate that while known eukaryotic PPCDCs are homotrimers, the active yeast enzyme is a heterotrimer which consists of Ykl088w and Hal3/Vhs3 monomers that separately provides two essential catalytic residues. Our results unveil Hal3/Vhs3 as moonlighting proteins, involved in both CoA biosynthesis and protein phosphatase regulation.
Nota: Premi a l'excel·lència investigadora. 2010
Drets: Tots els drets reservats
Llengua: Anglès.
Document: article ; altres ; acceptedVersion
Matèria: PREI 2010
Publicat a: Nature Chemical Biology, Vol. 5, Núm. 12 (2009) , p. 920-928, ISSN 1552-4469

DOI: 10.1038/nchembio.243

32 p, 2.8 MB

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