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2‐oxoglutarate‐Fe(II)‐dependent dioxygenase regulates degradation of nuclear sterol regulatory element binding protein in fission yeast

Sre1, the fission yeast Sterol Regulatory Element Binding Protein (SREBP), is a membrane‐bound transcription factor that monitors oxygen‐dependent sterol synthesis as a measure of oxygen availability, thereby controlling adaptation to low oxygen. When sterol synthesis decreases in the absence of oxygen, Sre1 is proteolytically cleaved, allowing the N‐terminal transcription factor domain to activate gene expression in the nucleus. To determine whether oxygen can directly regulate the activity of nuclear Sre1, we generated a yeast strain expressing a truncated nuclear form of the Sre1 transcription factor (Sre1N). Sre1N levels increased under low oxygen and in the presence of inhibitors of 2‐oxoglutarate (OG)‐Fe(II)‐dependent dioxygenases. We identified a 2‐OG‐Fe(II) dioxygenase, Ofd1, that accelerated the degradation of Sre1N in the presence of oxygen. These results support a model in which Ofd1 controls the turnover of the cleaved, nuclear form of Sre1, allowing oxygen to regulate Sre1 activity directly through a 2‐OG‐Fe(II)‐dependent dioxygenase.