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Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w in yeast CoA biosynthesis

Reference: Nat Chem Biol. 2009 Dec;5(12):920-8. Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w in yeast CoA biosynthesis
Authors: Amparo Ruiz1,4,7, Asier González1,2,7, Ivan Muñoz1,5, Raquel Serrano1,6, J Albert Abrie3, Erick Strauss3 and Joaquín Ariño1,2
1. Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, Spain.
2. Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Barcelona, Spain.
3. Department of Biochemistry, Stellenbosch University, Stellenbosch, South Africa.
4. Present address: Department of Genetics and Development and Department of Microbiology and Immunology, Columbia University, New York, New York, USA.
5. Present address: Medical Research Council Protein Phosphorylation Unit, Sir James Black Centre, University of Dundee, Dundee, Scotland, UK.
6. Present address: Department of Biological Sciences, Stanford University, Stanford, California, USA.
7. These authors contributed equally to this work.
Summary: Unlike most other organisms, the essential five-step coenzyme A biosynthetic pathway has not been fully resolved in yeast. Specifically, the genes encoding the phosphopantothenoylcysteine decarboxylase (PPCDC) activity still remain unidentified. Sequence homology analyses suggest three candidates—Ykl088w, Hal3 and Vhs3—as putative PPCDC enzymes in Saccharomyces cerevisiae. Notably, 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 and 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 that consists of Ykl088w and Hal3/Vhs3 monomers that separately provides two essential catalytic residues. Our results unveil Hal3 and Vhs3 as moonlighting proteins involved in both CoA biosynthesis and protein phosphatase regulation.
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REFERENCIA DEL GRUPO Y/O INVESTIGADOR
El Grupo de Biología Molecular de Levaduras se estableció en la UAB a principios de 1990. Su investigación se ha centrado principalmente en el estudio de la respuesta a estrés mediante procesos de fosfo-desfosforilación, con especial énfasis en las Ser/Thr proteína fosfatasas, habiendo descubierto y caracterizado numerosas fosfatasas de diversos organismos. Su modelo de estudio preferente es la levadura Saccharomyces cerevisiae, cuyo genoma contribuyeron a secuenciar por completo.


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