@prefix prodottidellaricerca: . @prefix istituto: . @prefix prodotto: . istituto:CDS015 prodottidellaricerca:prodotto prodotto:ID12834 . @prefix pubblicazioni: . @prefix unitaDiPersonaleInterno: . unitaDiPersonaleInterno:MATRICOLA33008 pubblicazioni:autoreCNRDi prodotto:ID12834 . @prefix modulo: . modulo:ID2562 prodottidellaricerca:prodotto prodotto:ID12834 . @prefix rdf: . prodotto:ID12834 rdf:type prodotto:TIPO1101 . @prefix retescientifica: . prodotto:ID12834 rdf:type retescientifica:ProdottoDellaRicerca . @prefix rdfs: . prodotto:ID12834 rdfs:label "Pleiotropic effects of the yeast Sal1 and Aac2 carriers on mitochondrial function via an activity distinct from adenine nucleotide transport (Articolo in rivista)"@en . @prefix xsd: . prodotto:ID12834 pubblicazioni:anno "2008-01-01T00:00:00+01:00"^^xsd:gYear . @prefix skos: . prodotto:ID12834 skos:altLabel "
Kucejova B; Li L; Wang X; Giannattasio S; Chen XJ (2008)
Pleiotropic effects of the yeast Sal1 and Aac2 carriers on mitochondrial function via an activity distinct from adenine nucleotide transport
in Molecular genetics and genomics (Print)
"^^rdf:HTML ; pubblicazioni:autori "Kucejova B; Li L; Wang X; Giannattasio S; Chen XJ"^^xsd:string ; pubblicazioni:paginaInizio "25"^^xsd:string ; pubblicazioni:paginaFine "39"^^xsd:string ; pubblicazioni:numeroVolume "280"^^xsd:string . @prefix ns11: . prodotto:ID12834 pubblicazioni:rivista ns11:ID58704 ; skos:note "ISI Web of Science (WOS)"^^xsd:string ; pubblicazioni:affiliazioni "CNR, Istituto di Biomembrane e Bioenergetica, Bari, Italy;\nDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse NY, USA;\nDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dalla TX, USA."^^xsd:string ; pubblicazioni:titolo "Pleiotropic effects of the yeast Sal1 and Aac2 carriers on mitochondrial function via an activity distinct from adenine nucleotide transport"^^xsd:string ; prodottidellaricerca:abstract "In Saccharomyces cerevisiae, SAL1 encodes a Ca(2+)-binding mitochondrial carrier. Disruption of SAL1 is synthetically lethal with the loss of a specific function associated with the Aac2 isoform of the ATP/ADP translocase. This novel activity of Aac2 is defined as the V function (for Viability of aac2 sal1 double mutant), which is independent of the ATP/ADP exchange activity required for respiratory growth (the R function). We found that co-inactivation of SAL1 and AAC2 leads to defects in mitochondrial translation and mitochondrial DNA (mtDNA) maintenance. Additionally, sal1Delta exacerbates the respiratory deficiency and mtDNA instability of ggc1Delta, shy1Delta and mtg1Delta mutants, which are known to reduce mitochondrial protein synthesis or protein complex assembly. The V function is complemented by the human Short Ca(2+)-binding Mitochondrial Carrier (SCaMC) protein, SCaMC-2, a putative ATP-Mg/P(i) exchangers on the inner membrane. However, mitochondria lacking both Sal1p and Aac2p are not depleted of adenine nucleotides. The Aac2(R252I) and Aac2(R253I) variants mutated at the R252-254 triplet critical for nucleotide transport retain the V function. Likewise, Sal1p remains functionally active when the R479I and R481I mutations were introduced into the structurally equivalent R479-T480-R481 motif. Finally, we found that the naturally occurring V(-)R(+) Aac1 isoform of adenine nucleotide translocase partially gains the V function at the expense of the R function by introducing the mutations P89L and A96 V. Thus, our data support the view that the V function is independent of adenine nucleotide transport associated with Sal1p and Aac2p and this evolutionarily conserved activity affects multiple processes in mitochondria."@en ; prodottidellaricerca:prodottoDi modulo:ID2562 , istituto:CDS015 ; pubblicazioni:autoreCNR unitaDiPersonaleInterno:MATRICOLA33008 . @prefix parolechiave: . prodotto:ID12834 parolechiave:insiemeDiParoleChiave . ns11:ID58704 pubblicazioni:rivistaDi prodotto:ID12834 . parolechiave:insiemeDiParoleChiaveDi prodotto:ID12834 .