Structural highlights
Publication Abstract from PubMed
Fission yeast protein Sre1, the homolog of the mammalian sterol regulatory element-binding protein (SREBP), is a hypoxic transcription factor required for sterol homeostasis and low-oxygen growth. Nro1 regulates the stability of the N-terminal transcription factor domain of Sre1 (Sre1N) by inhibiting the action of the prolyl 4-hydroxylase-like Ofd1 in an oxygen-dependent manner. The crystal structure of Nro1 determined at 2.2 A resolution shows an all-alpha-helical fold that can be divided into two domains: a small N-terminal domain, and a larger C-terminal HEAT-repeat domain. Follow-up studies showed that Nro1 defines a new class of nuclear import adaptor that functions both in Ofd1 nuclear localization and in the oxygen-dependent inhibition of Ofd1 to control the hypoxic response.
The hypoxic regulator of sterol synthesis nro1 is a nuclear import adaptor.,Yeh TL, Lee CY, Amzel LM, Espenshade PJ, Bianchet MA Structure. 2011 Apr 13;19(4):503-14. PMID:21481773[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yeh TL, Lee CY, Amzel LM, Espenshade PJ, Bianchet MA. The hypoxic regulator of sterol synthesis nro1 is a nuclear import adaptor. Structure. 2011 Apr 13;19(4):503-14. PMID:21481773 doi:10.1016/j.str.2011.01.017
