In:
Molecular Microbiology, Wiley, Vol. 92, No. 2 ( 2014-04), p. 246-257
Abstract:
The main peroxiredoxin in S chizosaccharomyces pombe , Tpx 1, is important to sustain aerobic growth, and cells lacking this protein are only able to grow on solid plates under anaerobic conditions. We have found that deletion of the gene coding for thioredoxin reductase, trr1 , is a suppressor of the sensitivity to aerobic growth of Δ tpx1 cells, so that cells lacking both proteins are able to grow on solid plates in the presence of oxygen. We have investigated this suppression effect, and determined that it depends on the presence of catalase, which is constitutively expressed in Δ trr1 cells in a transcription factor Pap 1‐dependent manner. A complete characterization of the repertoire of hydrogen peroxide scavenging activities in fission yeast suggests that Tpx 1 is the only enzyme with sufficient sensitivity for peroxides and cellular abundance as to control the low levels produced during aerobic growth, catalase being the next barrier of detoxification when the steady‐state levels of peroxides are increased in Δ tpx1 cells. Gpx 1, the only glutathione peroxidase encoded by the S . pombe genome, only has a minor secondary role when extracellular peroxides are added. Our study proposes non‐overlapping roles for the different hydrogen peroxide scavenging activities of this eukaryotic organism.
Type of Medium:
Online Resource
ISSN:
0950-382X
,
1365-2958
DOI:
10.1111/mmi.2014.92.issue-2
Language:
English
Publisher:
Wiley
Publication Date:
2014
detail.hit.zdb_id:
1501537-3
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