Antonie van Leeuwenhoek

, Volume 92, Issue 4, pp 463–472

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

Original Paper

DOI: 10.1007/s10482-007-9174-2

Cite this article as:
López-Mirabal, H.R. & Winther, J.R. Antonie van Leeuwenhoek (2007) 92: 463. doi:10.1007/s10482-007-9174-2

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°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.

Keywords

4,4′-dipyridyl disulfideendoplasmic reticulumGSH-GSSG redox buffer

Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • H. Reynaldo López-Mirabal
    • 1
    • 2
  • Jakob R. Winther
    • 1
    • 2
  1. 1.Carlsberg LaboratoryCopenhagen ValbyDenmark
  2. 2.Department of Biochemistry, Institute of Molecular BiologyAugust Krogh BuildingCopenhagenDenmark