| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3399032 | Current Opinion in Microbiology | 2015 | 7 Pages |
•Prolyl 4-hydroxylases are evolutionarily conserved O2 sensors.•Skp1 hydroxylation/glycosylation promotes SCF ubiquitin ligase assembly in protists.•HIF regulates transcriptional responses to hypoxia in animals.•Toxoplasma growth at low O2 requires SKP1 hydroxylation/glycosylation and host HIF.•Decreased O2 availability reduces trypanosome virulence gene expression.
Cells must know the local levels of available oxygen and either adapt accordingly or relocate to more favorable environments. Prolyl 4-hydroxylases (P4Hs) are emerging as universal cellular oxygen sensors. In animals, these oxygen sensors respond to decreased oxygen availability by up-regulating hypoxia-inducible transcription factors. In protozoa, the P4Hs appear to activate E3-SCF ubiquitin ligase complexes via a glycosylation-dependent mechanism, potentially to turn over their proteomes. Intracellular parasites are impacted by both types of oxygen-sensing pathways. Since parasites are exposed to diverse oxygen tensions during their life cycles, this review identifies emerging oxygen-sensing mechanisms and discusses how these mechanisms probably contribute to the regulation of unicellular eukaryotes.
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