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Orientation of aromatic residues in amyloid cores: Structural insights into prion fiber diversity

Author(s)
Reymer, Anna; Frederick, Kendra K.; Rocha, Sandra; Beke-Somfai, Tamas; Kitts, Catherine C.; Lindquist, Susan; Norden, Bengt; ... Show more Show less
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Abstract
Structural conversion of one given protein sequence into different amyloid states, resulting in distinct phenotypes, is one of the most intriguing phenomena of protein biology. Despite great efforts the structural origin of prion diversity remains elusive, mainly because amyloids are insoluble yet noncrystalline and therefore not easily amenable to traditional structural-biology methods. We investigate two different phenotypic prion strains, weak and strong, of yeast translation termination factor Sup35 with respect to angular orientation of tyrosines using polarized light spectroscopy. By applying a combination of alignment methods the degree of fiber orientation can be assessed, which allows a relatively accurate determination of the aromatic ring angles. Surprisingly, the strains show identical average orientations of the tyrosines, which are evenly spread through the amyloid core. Small variations between the two strains are related to the local environment of a fraction of tyrosines outside the core, potentially reflecting differences in fibril packing.
Date issued
2014-12
URI
http://hdl.handle.net/1721.1/97422
Department
Massachusetts Institute of Technology. Department of Biology; Whitehead Institute for Biomedical Research
Journal
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences (U.S.)
Citation
Reymer, Anna, Kendra K. Frederick, Sandra Rocha, Tamas Beke-Somfai, Catherine C. Kitts, Susan Lindquist, and Bengt Norden. “Orientation of Aromatic Residues in Amyloid Cores: Structural Insights into Prion Fiber Diversity.” Proceedings of the National Academy of Sciences 111, no. 48 (November 17, 2014): 17158–17163.
Version: Final published version
ISSN
0027-8424
1091-6490

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