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|Title:||Consequences of IkappaB alpha hydroxylation by the factor inhibiting HIF (FIH)|
|Citation:||FEBS Letters, 2010; 584(23):4725-4730|
|Publisher:||Elsevier Science BV|
|Ingrid L. Devries, Rachel J. Hampton-Smith, Melinda M. Mulvihill, Vera Alverdi, Daniel J. Peet and Elizabeth A. Komives|
|Abstract:||The factor inhibiting HIF-1 (FIH-1) hydroxylates many ankyrin repeat-containing proteins including IκBα. It is widely speculated that hydroxylation of IκBα has functional consequences, but the effects of hydroxylation have not been demonstrated. We prepared hydroxylated IκBα and compared it to the unhydroxylated protein. Urea denaturation and amide H/D exchange experiments showed no change in the “foldedness” upon hydroxylation. Surface plasmon resonance measurements of binding to NFκB showed no difference in the NFκB binding kinetics or thermodynamics. Ubiquitin-independent proteasomal degradation experiments showed no difference in the half-life of the protein. Thus, it appears that hydroxylation of IκBα by FIH-1 is inconsequential, at least for the functions we could assay in vitro.|
|Keywords:||Hypoxia-inducible factor; Ankyrin repeat; Post-translational modification; Protein folding; Proteasome degradation|
|Rights:||Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.|
|Appears in Collections:||Molecular and Biomedical Science publications|
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