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Functional complementation of yeast cytosolic pyrophosphatase by bacterial and plant H -translocating pyrophosphatases

Opened Access Functional complementation of yeast cytosolic pyrophosphatase by bacterial and plant H -translocating pyrophosphatases
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Autor: Losada Villasante, Manuel
Pérez Castiñeira, José Román
López Marqués, Rosa Laura
Villalba Montoro, José Manuel
Serrano Delgado, Aurelio
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2002
Publicado en: Proceedings of the National Academy of Sciences of the United States of America, 99(25), 15914–15919
Tipo de documento: Artículo
Resumen: Two types of proteins that hydrolyze inorganic pyrophosphate (PPi), very different in both amino acid sequence and structure, have been characterized to date: soluble and membrane-bound proton-pumping pyrophosphatases (sPPases and H+-PPases, respectively). sPPases are ubiquitous proteins that hydrolyze PPi releasing heat, whereas H+-PPases, so far unidentified in animal and fungal cells, couple the energy of PPi hydrolysis to proton movement across biological membranes. The budding yeast Saccharomyces cerevisiae has two sPPases that are located in the cytosol and in the mitochondria. Previous attempts to knock out the gene coding for a cytosolic sPPase (IPP1) have been unsuccessful, thus suggesting that this protein is essential for growth. Here, we describe the generation of a conditional S. cerevisiae mutant (named YPC-1) whose functional IPP1 gene is under the control of a galactose-dependent promoter. Thus, YPC-1 cells become growth arrested in glucose but they regain the ability ...
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Tamaño: 246.1Kb
Formato: PDF

URI: http://hdl.handle.net/11441/26079

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