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Articles 42 records found  beginprevious14 - 23nextend  jump to record: Search took 0.02 seconds. 
14.
22 p, 7.3 MB Yeast Ppz1 protein phosphatase toxicity involves the alteration of multiple cellular targets / Velázquez, Diego (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Albacar, Marcel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Zhang, Chunyi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Calafí, Carlos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; López Malo, María (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Torres Torronteras, Javier (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; Martí, Ramón 1915-1994 (Hospital Universitari Vall d'Hebron. Institut de Recerca) ; Kovalchuk, Sergey I. (University of Southern Denmark. Department of Biochemistry and Molecular Biology) ; Pinson, Benoit (Centre National de la Recherche Scientifique (França)) ; Jensen, Ole N. (University of Southern Denmark. Department of Biochemistry and Molecular Biology) ; Daignan-Fornier, Bertrand (Centre National de la Recherche Scientifique (França)) ; Casamayor Gracia, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Control of the protein phosphorylation status is a major mechanism for regulation of cellular processes, and its alteration often lead to functional disorders. Ppz1, a protein phosphatase only found in fungi, is the most toxic protein when overexpressed in Saccharomyces cerevisiae. [...]
2020 - 10.1038/s41598-020-72391-y
Scientific reports, Vol. 10 (September 2020) , art. 15613  
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15.
17 p, 3.5 MB The N-Terminal Region of Yeast Protein Phosphatase Ppz1 Is a Determinant for Its Toxicity / Calafi Pascual, Carlos Alberto (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; López-Malo, María (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Albacar, Marcel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Casamayor Gracia, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
The Ppz enzymes are Ser/Thr protein phosphatases present only in fungi that are characterized by a highly conserved C-terminal catalytic region, related to PP1c phosphatases, and a more divergent N-terminal extension. [...]
2020 - 10.3390/ijms21207733
International journal of molecular sciences, Vol. 21, Núm. 20 (October 2020) , art. 7733  
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16.
69 p, 3.2 MB Overexpression of budding yeast protein phosphatase Ppz1 impairs translation / Calafí, Carlos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; López-Malo, María (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Velázquez, Diego (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Zhang, Chunyi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Fernández-Fernández, José (Universidad de Sevilla. Departamento de Genética) ; Rodríguez-Galán, Olga (Universidad de Sevilla. Departamento de Genética) ; de la Cruz, Jesús (Universidad de Sevilla. Departamento de Genética) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Casamayor Gracia, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
The Ser/Thr protein phosphatase Ppz1 from Saccharomyces cerevisiae is the best characterized member of a family of enzymes only found in fungi. Ppz1 is regulated in vivo by two inhibitory subunits, Hal3 and Vhs3, which are moonlighting proteins also involved in the decarboxylation of the 4-phosphopantothenoylcysteine (PPC) intermediate required for coenzyme A biosynthesis. [...]
2020 - 10.1016/j.bbamcr.2020.118727
Biochimica et Biophysica Acta - Molecular Cell Research, Vol. 1867, Issue 8 (August 2020) , art. 118727  
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17.
37 p, 10.2 MB Cryptococcus neoformans can form titan-like cells in vitro in response to multiple signals / Trevijano-Contador, Núria (Centro Nacional de Microbiología (Espanya)) ; Oliveira, Haroldo César de (Universidade Estadual Paulista (UNESP). Departamento de Análises Clínicas) ; García-Rodas, Rocío (Centro Nacional de Microbiología (Espanya)) ; Rossi, Suélen Andreida (Centro Nacional de Microbiología (Espanya)) ; Llorente Muñoz, Irene (Centro Nacional de Microbiología (Espanya)) ; Zaballos, Ángel (Instituto de Salud Carlos III) ; Janbon, Guilhem (Institut Pasteur. Département de Mycologie) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Zaragoza, Óscar (Centro Nacional de Microbiología (Espanya)) ; Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí"
Cryptococcus neoformans is an encapsulated pathogenic yeast that can change the size of the cells during infection. In particular, this process can occur by enlarging the size of the capsule without modifying the size of the cell body, or by increasing the diameter of the cell body, which is normally accompanied by an increase of the capsule too. [...]
2018 - 10.1371/journal.ppat.1007007
PLOS pathogens, Vol. 14 issue 5 (2018) , art. e1007007  
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18.
12 p, 2.4 MB Mutations at the hydrophobic core affect Hal3 trimer stability, reducing its Ppz1 inhibitory capacity but not its PPCDC moonlighting function / Santolaria Bello, Carlos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Velázquez, Diego (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Strauss, Erick (Stellenbosch University. Department of Biochemistry) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
S. cerevisiae Hal3 (ScHal3) is a moonlighting protein that, is in its monomeric state, regulates the Ser/Thr protein phosphatase Ppz1, but also joins ScCab3 (and in some instances the Hal3 paralog Vhs3) to form an unusual heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme. [...]
2018 - 10.1038/s41598-018-32979-x
Scientific reports, Vol. 8 (2018) , art. 14701  
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19.
19 p, 4.0 MB Protein phosphatase Ppz1 is not regulated by a hal3-like protein in plant pathogen ustilago maydis / Zhang, Chunyi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; de la Torre, Antonio. (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Biología Funcional y Genómica) ; Pérez Martín, José (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Biología Funcional y Genómica) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Ppz enzymes are type-1 related Ser/Thr protein phosphatases that are restricted to fungi. In S. cerevisiae and other fungi, Ppz1 is involved in cation homeostasis and is regulated by two structurally-related inhibitory subunits, Hal3 and Vhs3, with Hal3 being the most physiologically relevant. [...]
2019 - 10.3390/ijms20153817
International journal of molecular sciences, Vol. 20, issue 15 (2019) , art. 3817  
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20.
14 p, 1.8 MB The yeast Aft2 transcription factor determines selenite toxicity by controlling the low affinity phosphate transport system / Pérez-Sampietro, Maria (Universitat de Lleida. Departament de Ciències Mèdiques Bàsiques) ; Serra Cardona, Albert (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Canadell, David (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Casas, Celia (Universitat de Lleida. Departament de Ciències Mèdiques Bàsiques) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Herrero, Enrique (Universitat de Lleida. Departament de Ciències Mèdiques Bàsiques)
The yeast Saccharomyces cerevisiae is employed as a model to study the cellular mechanisms of toxicity and defense against selenite, the most frequent environmental selenium form. We show that yeast cells lacking Aft2, a transcription factor that together with Aft1 regulates iron homeostasis, are highly sensitive to selenite but, in contrast to aft1 mutants, this is not rescued by iron supplementation. [...]
2016 - 10.1038/srep32836
Scientific reports, Vol. 6 (2016) , art. 32836  
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21.
14 p, 1.6 MB The effector AWR5 from the plant pathogen Ralstonia solanacearum is an inhibitor of the TOR signalling pathway / Popa, Crina (Centre de Recerca en Agrigenòmica) ; Liang, Li (Centre de Recerca en Agrigenòmica) ; Gil, Sergio (Universitat de Barcelona. Departament de Genètica) ; Tatjer, Laura (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Hashii, Keisuke (Kagawa University. Laboratory of Applied Molecular and Cell Biology) ; Tabuchi, Mitsuaki (Kagawa University. Laboratory of Applied Molecular and Cell Biology) ; Sánchez Coll, Núria (Centre de Recerca en Agrigenòmica) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Valls, Marc (Centre de Recerca en Agrigenòmica)
Bacterial pathogens possess complex type III effector (T3E) repertoires that are translocated inside the host cells to cause disease. However, only a minor proportion of these effectors have been assigned a function. [...]
2016 - 10.1038/srep27058
Scientific reports, Vol. 6 (2016) , art. 27058  
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22.
14 p, 2.9 MB The inhibitory mechanism of Hal3 on the yeast Ppz1 phosphatase : A mutagenesis analysis / Molero Merinero, Cristina (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Casado Vázquez, Carlos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
The Ser/Thr protein phosphatase (PPase) Ppz1 is an enzyme related to the ubiquitous type-1 PPases (PP1c) but found only in fungi. It is regulated by an inhibitory subunit, Hal3, which binds to its catalytic domain. [...]
2017 - 10.1038/s41598-017-09360-5
Scientific reports, Vol. 7 (2017) , art. 8819  
Detailed record - Creative Commons
23.
12 p, 472.1 KB Adaptation to potassium starvation of wild-type and K⁺-transport mutant (trk1,2) of Saccharomyces cerevisiae : 2-dimensional gel electrophoresis-based proteomic approach / Gelis, Samuel (Universidad de Córdoba. Departamento de Microbiología) ; Curto Rubio, Miguel (Universidad de Córdoba. Departamento de Bioquímica y Biología Molecular) ; Valledor, Luís (Universität Wien. Department Molekulare Systembiologie) ; González Seviné, Asier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ariño Carmona, Joaquín (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Jorrín, Jesús (Universidad de Córdoba. Departamento de Bioquímica y Biología Molecular) ; Ramos, José (Universidad de Córdoba. Departamento de Microbiología)
Saccharomyces cerevisiae wild-type (BY4741) and the corresponding mutant lacking the plasma membrane main potassium uptake systems (trk1,trk2) were used to analyze the consequences of K starvation following a proteomic approach. [...]
2012 - 10.1002/mbo3.23
MicrobiologyOpen, Vol. 1, issue 2 (June 2012) , p. 182-193  
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