Proteomics

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Tpo1‐mediated spermine and spermidine export controls cell cycle delay and times antioxidant protein expression during the oxidative stress response


ABSTRACT: Cells counteract oxidative stress by altering metabolism, cell cycle and gene expression. However, the mechanisms that coordinate these adaptations are only marginally understood. Here we provide evidence that timing of these responses in yeast requires export of the polyamines spermidine and spermine. We show that during hydrogen peroxide (H2O2) exposure, the polyamine transporter Tpo1 controls spermidine and spermine concentrations and mediates induction of antioxidant proteins, including Hsp70, Hsp90, Hsp104 and Sod1. Moreover, Tpo1 determines a cell cycle delay during adaptation to increased oxidant levels, and affects H2O2 tolerance. Thus, central components of the stress response are timed through Tpo1‐controlled polyamine export.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Jakob Vowinckel  

LAB HEAD: Markus Ralser

PROVIDER: PXD013373 | Pride | 2019-06-10

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
AK_Spermine_new_SET11.wiff Wiff
AK_Spermine_new_SET11.wiff.scan Wiff
AK_Spermine_new_SET110.wiff Wiff
AK_Spermine_new_SET110.wiff.scan Wiff
AK_Spermine_new_SET111.wiff Wiff
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Publications


Both single and multicellular organisms depend on anti-stress mechanisms that enable them to deal with sudden changes in the environment, including exposure to heat and oxidants. Central to the stress response are dynamic changes in metabolism, such as the transition from the glycolysis to the pentose phosphate pathway-a conserved first-line response to oxidative insults<sup>1,2</sup>. Here we report a second metabolic adaptation that protects microbial cells in stress situations. The role of th  ...[more]

Publication: 1/2

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