» Articles » PMID: 16283393

Exogenous Manganous Ion at Millimolar Levels Rescues All Known Dioxygen-sensitive Phenotypes of Yeast Lacking CuZnSOD

Overview
Publisher Springer
Specialty Biochemistry
Date 2005 Nov 12
PMID 16283393
Citations 35
Authors
Affiliations
Soon will be listed here.
Abstract

Yeasts lacking copper-zinc superoxide dismutase (sod1Delta) exhibit a broad range of phenotypes, many of which can be rescued by growth in the presence of high levels of ionic manganese. We undertook a comprehensive survey of the effects of manganese on wild-type and sod1Delta yeasts and found that 5 mM Mn2+ rescued all known growth-related phenotypes, such as slow growth in air, temperature sensitivity, specific amino acid auxotrophies, no growth in high oxygen, poor growth in nonfermentable carbon sources, and decreased stationary-phase survival. Iron-related phenotypes-elevated electron paramagnetic resonance detectable ("free") iron, decreased aconitase activity, and fragmenting vacuoles-as well as zinc sensitivity were also rescued. The activity of manganese superoxide dismutase remained constant or was reduced when the yeasts were grown in the presence of MnCl2, indicating that induction of this alternative superoxide dismutase is not the explanation. In contrast to MnCl2 treatment, addition of two manganese-containing superoxide dismutase mimetic compounds to the growth medium did not provide any rescue of sod1Delta yeast growth but rather had an sod1Delta-selective inhibitory effect at micromolar concentrations. Mechanisms by which ionic manganese can effect this rescue, while the mimetic compounds do not, are discussed.

Citing Articles

Characterization of ancestral Fe/Mn superoxide dismutases indicates their cambialistic origin.

Valenti R, Jablonska J, Tawfik D Protein Sci. 2022; 31(10):e4423.

PMID: 36173172 PMC: 9490801. DOI: 10.1002/pro.4423.


Impairment Mechanisms and Intervention Approaches for Aged Human Neuromuscular Junctions.

Badawi Y, Nishimune H Front Mol Neurosci. 2020; 13:568426.

PMID: 33328881 PMC: 7717980. DOI: 10.3389/fnmol.2020.568426.


Cu/Zn Superoxide Dismutase (Sod1) regulates the canonical Wnt signaling pathway.

Chandrasekharan B, Montllor-Albalate C, Colin A, Andersen J, Jang Y, Reddi A Biochem Biophys Res Commun. 2020; 534:720-726.

PMID: 33218686 PMC: 7785591. DOI: 10.1016/j.bbrc.2020.11.011.


Harnessing biocompatible chemistry for developing improved and novel microbial cell factories.

Liu J, Solem C, Jensen P Microb Biotechnol. 2019; 13(1):54-66.

PMID: 31386283 PMC: 6922530. DOI: 10.1111/1751-7915.13472.


Extra-mitochondrial Cu/Zn superoxide dismutase (Sod1) is dispensable for protection against oxidative stress but mediates peroxide signaling in Saccharomyces cerevisiae.

Montllor-Albalate C, Colin A, Chandrasekharan B, Bolaji N, Andersen J, Outten F Redox Biol. 2018; 21:101064.

PMID: 30576923 PMC: 6302037. DOI: 10.1016/j.redox.2018.11.022.


References
1.
Riley D . Functional mimics of superoxide dismutase enzymes as therapeutic agents. Chem Rev. 2001; 99(9):2573-88. DOI: 10.1021/cr980432g. View

2.
Weiss R, Flickinger A, Rivers W, Hardy M, Aston K, Ryan U . Evaluation of activity of putative superoxide dismutase mimics. Direct analysis by stopped-flow kinetics. J Biol Chem. 1993; 268(31):23049-54. View

3.
Wang Z, Porreca F, Cuzzocrea S, Galen K, Lightfoot R, Masini E . A newly identified role for superoxide in inflammatory pain. J Pharmacol Exp Ther. 2004; 309(3):869-78. DOI: 10.1124/jpet.103.064154. View

4.
Azevedo D, Tacnet F, Delaunay A, Rodrigues-Pousada C, Toledano M . Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling. Free Radic Biol Med. 2003; 35(8):889-900. DOI: 10.1016/s0891-5849(03)00434-9. View

5.
DAVIS C, Greger J . Longitudinal changes of manganese-dependent superoxide dismutase and other indexes of manganese and iron status in women. Am J Clin Nutr. 1992; 55(3):747-52. DOI: 10.1093/ajcn/55.3.747. View