Backbone resonance assignment of a proteolysis-resistant fragment in the oxygen-dependent degradation domain of the hypoxia inducible factor 1alpha

Abstract

Hypoxia-inducible factor 1α (HIF1α) is a transcription factor that plays a key role in the adaptation of cells to low oxygen stress and oxygen homeostasis. The oxygen-dependent degradation (ODD) domain of HIF1α responsible for the negative regulation of HIF1α in normoxia is intrinsically unfolded. Here, we carried out the backbone 1H, 15N, and 13C resonance assignment of a proteolysis-resistant fragment (residues 404-477) in the HIF1α ODD domain using NMR spectroscopy. About 98% (344/352) of all the 1HN, 15N, 13Cα, 13Cβ, and 13CO resonances were unambiguously assigned. The results will be useful for further investigation of the structural and dynamic states of the HIF1α ODD domain and its interaction with binding partners.