Caracterización funcional de los transportadores mitocondriales de la familia CaMC en "Saccharomyces cerevisiae"
Author
Cavero Martínez, SantiagoAdvisor
Satrustegui Gil Delgado, Jorgina
Entity
UAM. Departamento de Biología Molecular; Centro de Biología Molecular Severo Ochoa (CBM)Date
2004-06-21Subjects
Calcio-Transporte fisiológico-Tesis doctorales; Mitocondrias-Tesis doctorales; Biología y Biomedicina / BiologíaNote
Tesis Doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departamento de Biología Molecular, Fecha de lectura 21-06-2004Abstract
The transport of metabolites through the inner mitochondrial membrane is accomplished
by related proteins belonging to the initochondrial carrier superfamily (MCF). Over the last few
years a number of new MCs have been identified in yeast and man, including members of a
subfainily of calcium-binding mitochondrial carriers (CaMCs), with EF-hand calcium binding
motifs in their N-terminal domains. Aralarl and Citrin are two closely related human CaMCs
and we have recently found that they are isoforms of the mitochondrial aspanatelglutamate
carrier (AGC), regulated by calcium on the extemal face of the inner mitochondrial membrane.
Aralarl and Citriii are related to Agclp, a member of the CaMC subfamily in
Saccharomyces cerevisiae (902 smino acids, ORF YPR02lc), although its N-terminal domain
does not have EF-hand motifs. To gain insight into the physiological role of the Agclp we
disrupted the AGCl gene in S. cerevisiae and studied the resulting knock-out (agclA) cells
using conventional metabolic approaches as well as 1 3 n~ucle ar magnetic resonance (NMR).
Out results provide evideiice that Agclp is a yeast mitochondrial transporier for aspartate and
glutamate. It plays a role in nitrogen metabolism and ornithine synthesis in mitochondria, and is
required for the operation of the malate-aspartate redox shuttle in S. cerevisiae, a NADH shuttle
necessary for growth on acetate and fatiy acids as carbon sources.
Yn1083p, another member of the CaMC subfamily, is the orthologue of hiiman SCaMCs
(Short Calcium binditig Mitochondrial Carriers) whose transporier function is yet unknown, and
it harboun EF-hand motifs in its N-terminal domain. Using a yeast straiii where the YNLO83w
gene has been disrupted, we have shown that the mitochondrial carrier encoded by this gene is
involved in a carboxyatractyloside insensitive net adenine nucleotide transport in yeast
mitochondria. Thus, Yn1083p may have a transport activity similar to that of the caz*-regulated
ATP-Mg/Pi carrier identified in rat liver mitochondria. Moreover, we have shown that in yeasts
deticient in the three ADPIATP carrien, the disruption of YNL083w is letbal. These results
provide evidence that Yn1083p is involved in the transport of adenine iiucleotides into
mitochondria.
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