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Lina Patricia Barreto Parra

About Lina Patricia Barreto Parra:
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SEEK ID: https://fairdomhub.org/people/240

Location:  Spain

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ORCID: Not specified

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Project positions

TRANSLUCENT (Autonomous University of Barcelona)

Related items

TRANSLUCENT

Gene interaction networks and models of cation homeostasis in Saccharomyces cerevisiae

Programme: SysMO

Public web page: http://www.translucent-network.org/

Autonomous University of Barcelona

Country:  Spain

City: Not specified

Web page: Not specified

Metal Stress in Saccharomyces cerevisiae
TRANSLUCENT
No description specified

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Y_all27
TRANSLUCENT

13805988

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample016
TRANSLUCENT

BCN-RNAsample016

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

Y_all27
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13806089

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample002
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BCN-RNAsample002

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample025
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BCN-RNAsample025

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

Y_all27
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13806086

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

Y_all27
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Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample034
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Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample031
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Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample004
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BCN-RNAsample004

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

Y_all27
TRANSLUCENT

13806084

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample011
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BCN-RNAsample011

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

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BCN-RNAsample010

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample009
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Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

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BCN-RNAsample028

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

Y_all22
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Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

Y_all27
TRANSLUCENT

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Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample036
TRANSLUCENT

BCN-RNAsample036

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample005
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BCN-RNAsample005

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

BCN-RNAsample023
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BCN-RNAsample023

Creator: Lina Patricia Barreto Parra

Contributor: The JERM Harvester

1 hidden item
pH-BASED ESTIMATION OF YEAST ATPase ACTIVITY
TRANSLUCENT
No description specified

Creator: Lina Patricia Barreto Parra

Contributor: Lina Patricia Barreto Parra

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2 hidden items
Lack of main K(+) uptake systems in Saccharomyces cerevisiae cells affects yeast performance in both potassium-sufficient and potassium-limiting conditions
TRANSLUCENT

Abstract (Expand)

Abstract A new YNB medium containing very low concentrations of alkali metal cations has been developed to carry out experiments to study potassium homoeostasis. Physiological characterization of … Saccharomyces cerevisiae BY4741 strain and the corresponding mutant lacking the main potassium uptake systems (trk1 trk2) under potassium nonlimiting and limiting concentrations was performed, and novel important differences between both strains were found. At nonlimiting concentrations of KCl, the two strains had a comparable cell size and potassium content. Nevertheless, mutants were hyperpolarized, had lower pH and extruded fewer protons compared with the BY4741 strain. Upon transfer to K(+)-limiting conditions, cells of both strains became hyperpolarized and their cell volume and K(+) content diminished; however, the decrease was more relevant in BY4741. In low potassium, trk1 trk2 cells were not able to accomplish the cell cycle to the same extent as in BY4741. Moreover, K(+) limitation triggered a high-affinity K(+)/Rb(+) uptake process only in BY4741, with the highest affinity being reached as soon as 30 min after transfer to potassium-limiting conditions. By establishing basic cellular parameters under standard growth conditions, this work aims to establish a basis for the investigation of potassium homoeostasis at the system level.

Authors: Clara Navarrete, Silvia Petrezselyova, Lina Patricia Barreto Parra, José L Martínez, Jaromir Zahrádka, Joaquin Ariño, Hana Sychrova, Jose Ramos

Date Published: 25th May 2010

Journal: Not specified

Ref2, a regulatory subunit of the yeast protein phosphatase 1, is a novel component of cation homoeostasis
TRANSLUCENT

Abstract (Expand)

Maintenance of cation homoeostasis is a key process for any living organism. Specific mutations in Glc7, the essential catalytic subunit of yeast protein phosphatase 1, result in salt and alkaline pH … sensitivity, suggesting a role for this protein in cation homoeostasis. We screened a collection of Glc7 regulatory subunit mutants for altered tolerance to diverse cations (sodium, lithium and calcium) and alkaline pH. Among 18 candidates, only deletion of REF2 (RNA end formation 2) yielded increased sensitivity to these conditions, as well as to diverse organic toxic cations. The Ref2F374A mutation, which renders it unable to bind Glc7, did not rescue the salt-related phenotypes of the ref2 strain, suggesting that Ref2 function in cation homoeostasis is mediated by Glc7. The ref2 deletion mutant displays a marked decrease in lithium efflux, which can be explained by the inability of these cells to fully induce the Na+-ATPase ENA1 gene. The effect of lack of Ref2 is additive to that of blockage of the calcineurin pathway and might disrupt multiple mechanisms controlling ENA1 expression. ref2 cells display a striking defect in vacuolar morphogenesis, which probably accounts for the increased calcium levels observed under standard growth conditions and the strong calcium sensitivity of this mutant. Remarkably, the evidence collected indicates that the role of Ref2 in cation homoeostasis may be unrelated to its previously identified function in the formation of mRNA via the APT (for associated with Pta1) complex.

Authors: Jofre Ferrer-Dalmau, Asier González, Maria Platara, Clara Navarrete, José L Martínez, Lina Patricia Barreto Parra, Jose Ramos, Joaquin Ariño, Antonio Casamayor

Date Published: 24th Dec 2009

Journal: Biochem. J.

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