Orientation of aromatic residues in amyloid cores: Structural insights into prion fiber diversity
Journal article, 2014

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.

polarized light

tyrosine

prion proteins

Sup35 strains

linear dichroism

Author

Anna Reymer

Chalmers, Chemical and Biological Engineering, Physical Chemistry

K. K. Frederick

Howard Hughes Medical Institute

Whitehead Institute for Biomedical Research

Sandra Rocha

Chalmers, Chemical and Biological Engineering, Physical Chemistry

Tamas Beke-Somfai

Chalmers, Chemical and Biological Engineering, Physical Chemistry

Catherine Kitts

Chalmers, Chemical and Biological Engineering, Physical Chemistry

S. Lindquist

Massachusetts Institute of Technology (MIT)

Howard Hughes Medical Institute

Whitehead Institute for Biomedical Research

Bengt Nordén

Chalmers, Chemical and Biological Engineering, Physical Chemistry

Proceedings of the National Academy of Sciences of the United States of America

0027-8424 (ISSN) 1091-6490 (eISSN)

Vol. 111 48 17158-17163

Subject Categories

Physical Chemistry

DOI

10.1073/pnas.1415663111

More information

Latest update

4/11/2018