Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/62423
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Type: Journal article
Title: Consequences of IkappaB alpha hydroxylation by the factor inhibiting HIF (FIH)
Author: Devries, I.
Hampton-Smith, R.
Mulvihill, M.
Alverdi, V.
Peet, D.
Komives, E.
Citation: FEBS Letters, 2010; 584(23):4725-4730
Publisher: Elsevier Science BV
Issue Date: 2010
ISSN: 0014-5793
1873-3468
Statement of
Responsibility: 
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.
RMID: 0020101535
DOI: 10.1016/j.febslet.2010.10.060
Description (link): http://www.elsevier.com/wps/find/journaldescription.cws_home/506085/description#description
Appears in Collections:Molecular and Biomedical Science publications

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