yAP-1- and yAP-2-mediated, heat shock-induced transcriptional activation of the multidrug resistance ABC transporter genes in Saccharomyces cerevisiae

1996 ◽  
Vol 29 (2) ◽  
pp. 103-105 ◽  
Author(s):  
Kohji Miyahara ◽  
Dai Hirata ◽  
T. Miyakawa
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Multidrug Resistance ◽  
Heat Shock ◽  
Abc Transporter ◽  
Transcriptional Activation ◽  
Abc Transporter Genes

scholarly journals Vmr 1p is a novel vacuolar multidrug resistance ABC transporter in Saccharomyces cerevisiae

2010 ◽  
Vol 10 (7) ◽  
pp. 828-838 ◽  
Author(s):  
Donata Wawrzycka ◽  
Iwona Sobczak ◽  
Grzegorz Bartosz ◽  
Tomasz Bocer ◽  
Stanisław Ułaszewski ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Multidrug Resistance ◽  
Abc Transporter

scholarly journals Regulation of Thermotolerance by Stress-Induced Transcription Factors in Saccharomyces cerevisiae

2008 ◽  
Vol 7 (5) ◽  
pp. 783-790 ◽  
Author(s):  
Noritaka Yamamoto ◽  
Yuka Maeda ◽  
Aya Ikeda ◽  
Hiroshi Sakurai
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcription Factors ◽  
High Temperature ◽  
Heat Shock ◽  
Cell Growth ◽  
Rna Polymerase Ii ◽  
Transcriptional Activation ◽  
Target Genes ◽  
Recovery Period ◽  
Before And After

ABSTRACT The heat shock transcription factor Hsf1 and the general stress transcription factors Msn2 and Msn4 (Msn2/4) are major regulators of the heat shock response in Saccharomyces cerevisiae. Here, we show that transcriptional activation of their target genes, including HSP104, an antistress chaperone gene, is obligatory for thermotolerance. Although Hsf1 activity might be necessary before the exposure of cells to high temperature, severe heat shock induced the binding of hyperphosphorylated Hsf1 to its target promoters. However, promoter-bound, phosphorylated Hsf1 was inactive for transcription because RNA polymerase II was inactive at high temperatures. Rather, our results suggest that Hsf1 activates the transcription of most of its target genes during the recovery period following severe heat shock. This delayed upregulation by Hsf1, which would be induced by misfolded proteins that accumulate in severely heat-shocked cells, is required for the resumption of normal cell growth. In contrast, the factors Msn2/4 were not involved in the delayed upregulation of genes and were dispensable for cell growth during the recovery period, suggesting that they play a role before the exposure to high temperature. These results show that Hsf1 and Msn2/4 act differentially before and after exposure to extreme temperatures to ensure cell survival and growth.

Family business: the multidrug-resistance related protein (MRP) ABC transporter genes in Arabidopsis thaliana

Planta ◽  
2002 ◽  
Vol 216 (1) ◽  
pp. 107-119 ◽  
Author(s):  
Üner Kolukisaoglu ◽  
Lucien Bovet ◽  
Markus Klein ◽  
Thomas Eggmann ◽  
Markus Geisler ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Multidrug Resistance ◽  
Abc Transporter ◽  
Family Business ◽  
Related Protein ◽  
Abc Transporter Genes ◽  
Multidrug Resistance Related Protein

scholarly journals Mutational Disruption of Plasma Membrane Trafficking of Saccharomyces cerevisiae Yor1p, a Homologue of Mammalian Multidrug Resistance Protein

1999 ◽  
Vol 19 (4) ◽  
pp. 2998-3009 ◽  
Author(s):  
David J. Katzmann ◽  
Eric A. Epping ◽  
W. Scott Moye-Rowley
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Multidrug Resistance ◽  
Abc Transporter ◽  
Membrane Trafficking ◽  
Predicted Amino Acid Sequence ◽  
Multidrug Resistance Protein ◽  
Wild Type ◽  
Amino Terminal ◽  
Resistance Protein

ABSTRACT The ATP binding cassette (ABC) transporter protein Yor1p was identified on the basis of its ability to elevate oligomycin resistance when it was overproduced from a high-copy-number plasmid. Analysis of the predicted amino acid sequence of Yor1p indicated that this protein was a new member of a subfamily of ABC transporter proteins defined by the multidrug resistance protein (MRP). In this work, Yor1p is demonstrated to localize to the Saccharomyces cerevisiaeplasma membrane by both indirect immunofluorescence and biochemical fractionation studies. Several mutations were generated in the amino-terminal nucleotide binding domain (NBD1) of Yor1p to test if the high degree of sequence conservation in this region of the protein was important for function. Deletion of a phenylalanine residue at Yor1p position 670 led to a mutant protein that appeared to be retained in the endoplasmic reticulum (ER) and that was unstable. As shown by others, deletion of the analogous residue from a second mammalian MRP family member, the cystic fibrosis transmembrane conductance regulator (CFTR), also led to retention of this normally plasma membrane-localized protein in the ER. Changes in the spacing between or the sequences flanking functional motifs of Yor1p NBD1 led to defective trafficking or decreased activity of the mutant proteins. Analyses of the degradation of wild-type and ΔF670 Yor1p indicated that the half-life of ΔF670 Yor1p was dramatically shortened. While the vacuole was the primary site for turnover of wild-type Yor1p, degradation of ΔF670 Yor1p was found to be more complex with both proteasomal and vacuolar contributions.

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