Mañana, JUEVES, 24 DE ABRIL, el sistema se apagará debido a tareas habituales de mantenimiento a partir de las 9 de la mañana. Lamentamos las molestias.
Characterization of two second-site mutations preventing wild type protein aggregation caused by a dominant negative PMA1 mutant
Entidad
UAM. Departamento de BioquímicaEditor
Public Library of ScienceFecha de edición
2013-06-25Cita
10.1371/journal.pone.0067080
Plos One 8.6 (2013): e67080
ISSN
1932-6203 (online)DOI
10.1371/journal.pone.0067080Financiado por
This work was supported by the Spanish Ministerio de Ciencia e Innovación Grant BFU2008-04285Materias
Alleles; Amino Acid Sequence; Mutant Proteins; Proton-Translocating ATPases; Saccharomyces cerevisiae; Cell Membrane; MedicinaDerechos
© 2013 Eraso et al.Resumen
The correct biogenesis and localization of Pma1 at the plasma membrane is essential for yeast growth. A subset of PMA1 mutations behave as dominant negative because they produce aberrantly folded proteins that form protein aggregates, which in turn provoke the aggregation of the wild type protein. One approach to understand this dominant negative effect is to identify second-site mutations able to suppress the dominant lethal phenotype caused by those mutant alleles. We isolated and characterized two intragenic second-site suppressors of the PMA1-D378T dominant negative mutation. We present here the analysis of these new mutations that are located along the amino-terminal half of the protein and include a missense mutation, L151F, and an in-frame 12bp deletion that eliminates four residues from Cys409 to Ala412. The results show that the suppressor mutations disrupt the interaction between the mutant and wild type enzymes, and this enables the wild type Pma1 to reach the plasma membrane
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Google Scholar:Eraso Mazmela, Pilar
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Portillo Pérez, Francisco
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Mazón, María J.
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