The thiol oxidant dipyridyl disulfide can supply the PDI-Ero1p pathway with additional oxidative equivalents.

H Reynaldo López-Mirabal; Jakob R Winther

doi:10.1007/s10482-007-9174-2

The thiol oxidant dipyridyl disulfide can supply the PDI-Ero1p pathway with additional oxidative equivalents.

H Reynaldo López-Mirabal, Jakob R Winther

Biomolecular Sciences

6 Citations (Scopus)

Abstract

Membrane-permeant oxidants have become a standard tool for studying eukaryotic organisms because they affect the redox state and the redox regulation of different compartments. The ero1-1 mutant is temperature sensitive (37 degrees C) and cannot grow under anaerobic conditions. Low micromolar concentrations of the specific thiol-oxidant dipyridyl disulfide (DPS) rescue both these growth defects. Furthermore, the unfolded protein response (UPR) is slightly induced by a DPS treatment. We infer that DPS may change the redox state of important ER-proteins by GSH-oxidation in the ER or, more likely, by directly oxidizing these targets. Therefore, DPS may be useful in genetic studies dealing with unknown factors of the Ero1p-driven pathway. The ero1-1 mutation and the overproduction of Ero1p confer DPS-sensitivity that could be partially related to a more oxidized cytosolic GSH redox potential and the presence of reactive oxidative species (ROS) in the cell.
Udgivelsesdato: 2007-Nov

Original language	English
Journal	Antonie van Leeuwenhoek. International Journal of General and Molecular Microbiology
Volume	92
Issue number	4
Pages (from-to)	463-72
Number of pages	9
ISSN	0003-6072
DOIs	https://doi.org/10.1007/s10482-007-9174-2
Publication status	Published - 2007

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10.1007/s10482-007-9174-2

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title = "The thiol oxidant dipyridyl disulfide can supply the PDI-Ero1p pathway with additional oxidative equivalents.",

abstract = "Membrane-permeant oxidants have become a standard tool for studying eukaryotic organisms because they affect the redox state and the redox regulation of different compartments. The ero1-1 mutant is temperature sensitive (37 degrees C) and cannot grow under anaerobic conditions. Low micromolar concentrations of the specific thiol-oxidant dipyridyl disulfide (DPS) rescue both these growth defects. Furthermore, the unfolded protein response (UPR) is slightly induced by a DPS treatment. We infer that DPS may change the redox state of important ER-proteins by GSH-oxidation in the ER or, more likely, by directly oxidizing these targets. Therefore, DPS may be useful in genetic studies dealing with unknown factors of the Ero1p-driven pathway. The ero1-1 mutation and the overproduction of Ero1p confer DPS-sensitivity that could be partially related to a more oxidized cytosolic GSH redox potential and the presence of reactive oxidative species (ROS) in the cell. Udgivelsesdato: 2007-Nov",

author = "L{\'o}pez-Mirabal, {H Reynaldo} and Winther, {Jakob R}",

note = "Keywords: Anaerobiosis; Disulfides; Fungal Proteins; Genes, Essential; Glycoproteins; Heat; Oxidants; Protein Disulfide-Isomerase; Pyridines; Saccharomyces cerevisiae Proteins",

year = "2007",

doi = "10.1007/s10482-007-9174-2",

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T1 - The thiol oxidant dipyridyl disulfide can supply the PDI-Ero1p pathway with additional oxidative equivalents.

AU - López-Mirabal, H Reynaldo

AU - Winther, Jakob R

N1 - Keywords: Anaerobiosis; Disulfides; Fungal Proteins; Genes, Essential; Glycoproteins; Heat; Oxidants; Protein Disulfide-Isomerase; Pyridines; Saccharomyces cerevisiae Proteins

PY - 2007

Y1 - 2007

N2 - Membrane-permeant oxidants have become a standard tool for studying eukaryotic organisms because they affect the redox state and the redox regulation of different compartments. The ero1-1 mutant is temperature sensitive (37 degrees C) and cannot grow under anaerobic conditions. Low micromolar concentrations of the specific thiol-oxidant dipyridyl disulfide (DPS) rescue both these growth defects. Furthermore, the unfolded protein response (UPR) is slightly induced by a DPS treatment. We infer that DPS may change the redox state of important ER-proteins by GSH-oxidation in the ER or, more likely, by directly oxidizing these targets. Therefore, DPS may be useful in genetic studies dealing with unknown factors of the Ero1p-driven pathway. The ero1-1 mutation and the overproduction of Ero1p confer DPS-sensitivity that could be partially related to a more oxidized cytosolic GSH redox potential and the presence of reactive oxidative species (ROS) in the cell. Udgivelsesdato: 2007-Nov

AB - Membrane-permeant oxidants have become a standard tool for studying eukaryotic organisms because they affect the redox state and the redox regulation of different compartments. The ero1-1 mutant is temperature sensitive (37 degrees C) and cannot grow under anaerobic conditions. Low micromolar concentrations of the specific thiol-oxidant dipyridyl disulfide (DPS) rescue both these growth defects. Furthermore, the unfolded protein response (UPR) is slightly induced by a DPS treatment. We infer that DPS may change the redox state of important ER-proteins by GSH-oxidation in the ER or, more likely, by directly oxidizing these targets. Therefore, DPS may be useful in genetic studies dealing with unknown factors of the Ero1p-driven pathway. The ero1-1 mutation and the overproduction of Ero1p confer DPS-sensitivity that could be partially related to a more oxidized cytosolic GSH redox potential and the presence of reactive oxidative species (ROS) in the cell. Udgivelsesdato: 2007-Nov

U2 - 10.1007/s10482-007-9174-2

DO - 10.1007/s10482-007-9174-2

M3 - Journal article

C2 - 17564811

SN - 0003-6072

VL - 92

SP - 463

EP - 472

JO - Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology

JF - Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology

IS - 4

ER -