Rpl12p affects the transcription of the PHO pathway high-affinity inorganic phosphate transporters and repressible phosphatases

Yeast ◽  
2011 ◽  
Vol 28 (6) ◽  
pp. 481-493 ◽  
Author(s):  
Wen-Yo Tu ◽  
Yu-Chen Huang ◽  
Li-Fan Liu ◽  
Li-Hsueh Chang ◽  
Ming F. Tam
Keyword(s):  
Inorganic Phosphate ◽  
Phosphate Transporters ◽  
High Affinity ◽  
Pho Pathway

Effect of Non-Solubilizing SDS Concentrations on High Affinity Ca2+ Binding and Steady State Phosphorylation by Inorganic Phosphate of the Sarcoplasmic Reticulum ATPase

1989 ◽  
Vol 44 (1-2) ◽  
pp. 139-152 ◽  
Author(s):  
Elisabeth Fassold ◽  
Wilhelm Hasselbach ◽  
Bernd Küchler
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Inorganic Phosphate ◽  
Atp Hydrolysis ◽  
Mutual Exclusion ◽  
Chemical Properties ◽  
Cooperative Interaction ◽  
Hydrophobic Force ◽  
High Affinity ◽  
Binding Domains ◽  
Phosphorylation Domain

Abstract In this investigation low, non-solubilizing concentrations of the strong anionic detergent SDS were used to perturbate the interaction of Ca2+ and Pi with their respective binding domains on the sarcoplasmic reticulum Ca-transport ATPase. Rising SDS concentrations produce a two-step decline of Ca2+-dependent ATP hydrolysis. At pH 6.15, SDS differently affects high affinity Ca2+ binding and phosphorylation by inorganic phosphate and releases the “mutual exclusion” of these two ligand binding steps. The degree of uncoupling is considerably more pronounced in the presence of 20% Me2SO. The reduction of Ca2+ binding by SDS is demonstrated to be a result of decreased affinity of one of the two specific high affinity binding sites and of perturbation of their cooperative interaction. Higher SDS partially restores the original high Ca2+ affinity but not the cooperativity of binding. Phosphorylation exhibits a higher SDS sensitivity than Ca2+ binding: Increasing SDS competitively inhibits and then completely abolishes phosphoenzyme formation. Thus. SDS binds to the phosphorylation domain, evidently involving the Lys352 residue of the ATPase molecule; this is accompanied by a more unspecific concentration-dependent SDS effect, probably mediated by hydrophobic force, which, finally, suppresses phosphorylation. Me2SO does neither qualitatively affect the SDS-dependent chemical properties of the vesicular material nor the SDS-dependent perturbation of the investigated reaction steps.

Differential roles for the low-affinity phosphate transporters Pho87 and Pho90 in Saccharomyces cerevisiae

2011 ◽  
Vol 434 (2) ◽  
pp. 243-251 ◽  
Author(s):  
Ruben Ghillebert ◽  
Erwin Swinnen ◽  
Pepijn De Snijder ◽  
Bart Smets ◽  
Joris Winderickx
Keyword(s):  
Transport System ◽  
Nitrogen Starvation ◽  
Yeast Cells ◽  
Interacting Proteins ◽  
High Affinity ◽  
Pho Pathway ◽  
Pi Transport ◽  
Expression Of Genes ◽  
Pi Acquisition ◽  
Pi Starvation

When starved of Pi, yeast cells activate the PHO signalling pathway, wherein the Pho4 transcription factor mediates expression of genes involved in Pi acquisition, such as PHO84, encoding the high-affinity H+/Pi symporter. In contrast, transcription of PHO87 and PHO90, encoding the low-affinity H+/Pi transport system, is independent of phosphate status. In the present work, we reveal that, upon Pi starvation, these low-affinity Pi transporters are endocytosed and targeted to the vacuole. For Pho87, this process strictly depends on SPL2, another Pho4-dependent gene that encodes a protein known to interact with the N-terminal SPX domain of the transporter. In contrast, the vacuolar targeting of Pho90 upon Pi starvation is independent of both Pho4 and Spl2, although it still requires its SPX domain. Furthermore, both Pho87 and Pho90 are also targeted to the vacuole upon carbon-source starvation or upon treatment with rapamycin, which mimics nitrogen starvation, but although these responses are independent of PHO pathway signalling, they again require the N-terminal SPX domain of the transporters. These observations suggest that other SPX-interacting proteins must be involved. In addition, we show that Pho90 is the most important Pi transporter under high Pi conditions in the absence of a high-affinity Pi-transport system. Taken together, our results illustrate that Pho87 and Pho90 represent non-redundant Pi transporters, which are tuned by the integration of multiple nutrient signalling mechanisms in order to adjust Pi-transport capacity to the general nutritional status of the environment.

Inorganic phosphate transporters in cancer: Functions, molecular mechanisms and possible clinical applications

2018 ◽  
Vol 1870 (2) ◽  
pp. 291-298 ◽  
Author(s):  
Marco Antônio Lacerda-Abreu ◽  
Thais Russo-Abrahão ◽  
Robson de Queiroz Monteiro ◽  
Franklin David Rumjanek ◽  
José Roberto Meyer-Fernandes
Keyword(s):  
Inorganic Phosphate ◽  
Molecular Mechanisms ◽  
Clinical Applications ◽  
Phosphate Transporters

Research Article Isolation of high-affinity phosphate transporters SbPT1 AND SbPT2 in Sorghum bicolor and their characterization in contrasting genotypes

2021 ◽  
Vol 20 (2) ◽  
Author(s):  
M.J.V. de Vasconcelos ◽  
R.E. Schaffert ◽  
M.F. de Oliveira ◽  
A. Jain ◽  
J.E.F. Figueiredo ◽  
...  
Keyword(s):  
Phosphate Transporters ◽  
High Affinity ◽  
Research Article

scholarly journals Regulation of Cation-Coupled High-Affinity Phosphate Uptake in the Yeast Saccharomyces cerevisiae

2000 ◽  
Vol 182 (17) ◽  
pp. 5017-5019 ◽  
Author(s):  
Johanna Pattison-Granberg ◽  
Bengt L. Persson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Growth Phase ◽  
Phosphate Uptake ◽  
Phosphate Starvation ◽  
Fine Tuning ◽  
Yeast Saccharomyces Cerevisiae ◽  
Phosphate Transporters ◽  
High Affinity ◽  
Mutant Strains ◽  
Uptake Process

ABSTRACT Studies of the high-affinity phosphate transporters in the yeastSaccharomyces cerevisiae using mutant strains lacking either the Pho84 or the Pho89 permease revealed that the transporters are differentially regulated. Although both genes are induced by phosphate starvation, activation of the Pho89 transporter precedes that of the Pho84 transporter early in the growth phase in a way which may possibly reflect a fine tuning of the phosphate uptake process relative to the availability of external phosphate.

scholarly journals Expression analysis of putative high-affinity phosphate transporters in Chinese winter wheats

2002 ◽  
Vol 25 (10) ◽  
pp. 1325-1339 ◽  
Author(s):  
T. G. E. Davies ◽  
J. Ying ◽  
Q. Xu ◽  
Z. S. Li ◽  
J. Li ◽  
...  
Keyword(s):  
Expression Analysis ◽  
Phosphate Transporters ◽  
High Affinity
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