Structural highlights
Function[ETT1_SCHPO] Required for correct translation termination (By similarity). Positive regulator of the stability of the N-terminal transcription factor domain (Sre1N) of sre1 which is released from the membrane and enters the nucleus to activate hypoxic gene expression. Acts also as a direct inhibitor of ofd1. Functions probably by inhibiting the ability of the ofd1 to accelerate Sre1N degradation in absence of oxygen.[1] [2] Publication Abstract from PubMedFission 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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