a deubiquitylating complex required for neosynthesis of a yeast mitochondrial atp synthase subunitdeubiquitylating复杂neosynthesis所需的酵母线粒体atp合酶亚基.pdfVIP

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a deubiquitylating complex required for neosynthesis of a yeast mitochondrial atp synthase subunitdeubiquitylating复杂neosynthesis所需的酵母线粒体atp合酶亚基.pdf

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a deubiquitylating complex required for neosynthesis of a yeast mitochondrial atp synthase subunitdeubiquitylating复杂neosynthesis所需的酵母线粒体atp合酶亚基

A Deubiquitylating Complex Required for Neosynthesis of a Yeast Mitochondrial ATP Synthase Subunit 1 1¤a 3 1¤b Sophie Kanga , Delphine Bernard , Anne-Marie Mager-Heckel , Zoi Erpapazoglou , 2 2 ´ ´ 1 ` 1 3 Francesca Mattiroli , Titia K. Sixma , Sebastien Leon , Daniele Urban-Grimal , Ivan Tarassov , Rosine Haguenauer-Tsapis1* ´ 1 Institut Jacques Monod, CNRS, UMR7592, Univ Paris Diderot, Sorbonne Paris Cite, Paris, France, 2 Division of Biochemistry, Netherlands Cancer Institute, Amsterdam, The ´ ´ ´ ´ ´ Netherlands, 3 UMR 7156 Genetique Moleculaire, Genomique, Microbiologie (GMGM), Universite de Strasbourg - CNRS, Strasbourg, France Abstract The ubiquitin system is known to be involved in maintaining the integrity of mitochondria, but little is known about the role of deubiquitylating (DUB) enzymes in such functions. Budding yeast cells deleted for UBP13 and its close homolog UBP9 displayed a high incidence of petite colonies and slow respiratory growth at 37uC. Both Ubp9 and Ubp13 interacted directly with Duf1 (DUB-associated factor 1), a WD40 motif-containing protein. Duf1 activates the DUB activity of recombinant Ubp9 and Ubp13 in vitro and deletion of DUF1 resulted in the same respiratory phenotype as the deletion of both UBP9 and UBP13. We show that the mitochondrial defects of these mutants resulted from a strong decrease at 37uC in the de novo biosynthesis of