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Effects of the Iowa and Milano mutations on apolipoprotein A-I structure and dynamics determined by hydrogen exchange and mass spectrometry.

Abstract：

:The Iowa point mutation in apolipoprotein A-I (G26R) leads to a systemic amyloidosis condition, and the Milano mutation (R173C) is associated with hypoalphalipoproteinemia, a reduced plasma level of high-density lipoprotein. To probe the structural effects that lead to these outcomes, we used amide hydrogen-deuterium exchange coupled with a fragment separation/mass spectrometry analysis (HX MS). The Iowa mutation inserts an arginine residue into the nonpolar face of an α-helix that spans residues 7-44 and causes changes in structure and structural dynamics. This helix unfolds, and other helices in the N-terminal helix bundle domain are destabilized. The segment encompassing residues 116-158, largely unstructured in wild-type apolipoprotein A-I, becomes helical. The helix spanning residues 81-115 is destabilized by 2 kcal/mol, increasing the small fraction of time it is transiently unfolded to ≥1%, which allows proteolysis at residue 83 in vivo over time, releasing an amyloid-forming peptide. The Milano mutation situated on the polar face of the helix spanning residues 147-178 destabilizes the helix bundle domain only moderately, but enough to allow cysteine-mediated dimerization that leads to the altered functionality of this variant. These results show how the HX MS approach can provide a powerful means of monitoring, in a nonperturbing way and at close to amino acid resolution, the structural, dynamic, and energetic consequences of biologically interesting point mutations.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Chetty PS,Ohshiro M,Saito H,Dhanasekaran P,Lund-Katz S,Mayne L,Englander W,Phillips MC

doi

10.1021/bi300926j

subject

Has Abstract

pub_date

2012-11-06 00:00:00

pages

8993-9001

issue

44

eissn

0006-2960

issn

1520-4995

journal_volume

51

pub_type

杂志文章

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