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Asparagine beta-hydroxylation stabilizes the ankyrin repeat domain fold.

Leanne Kelly¹, Michael A McDonough, Mathew L Coleman

¹The Chemistry Research Laboratory and Oxford Centre for Integrative Systems Biology, University of Oxford, Oxford, UKOX1 3TA.

Molecular Biosystems

|December 17, 2008

Summary

Factor inhibiting hypoxia-inducible factor (FIH) hydroxylates ankyrin repeat domains (ARDs). This hydroxylation stabilizes the ARD protein structure in solution, suggesting a broader role for protein hydroxylation in cells.

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Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Ankyrin repeats (ARs) are prevalent structural motifs in eukaryotic proteins.
Factor inhibiting hypoxia-inducible factor (FIH) is known to hydroxylate asparagine residues in ankyrin repeat domains (ARDs).
The structural impact of this Asn-hydroxylation on ARDs remains largely uncharacterized.

Purpose of the Study:

To investigate the effect of FIH-mediated Asn-hydroxylation on the structure and stability of ankyrin repeat domains.
To confirm that consensus ARD proteins are substrates for FIH hydroxylation in vitro and in vivo.
To elucidate the role of hydroxylation in ARD protein function and stability.

Main Methods:

In vitro and in vivo assays to identify ARD proteins as FIH substrates.
X-ray diffraction analysis to determine ARD structure in crystalline states.
Biophysical techniques to assess ARD stability in solution.

Main Results:

Consensus ARD proteins were confirmed as FIH substrates both in vitro and in vivo.
X-ray diffraction showed no significant alteration in ARD conformation in the crystalline state post-hydroxylation.
Solution-based biophysical analyses revealed significant stabilization of the ARD fold upon hydroxylation.

Conclusions:

FIH-mediated hydroxylation of ARDs does not disrupt the canonical ARD fold.
Hydroxylation enhances the stability of ARD structures in solution.
Intracellular protein hydroxylation may be more widespread than previously assumed, potentially serving to stabilize protein domains.