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Title: Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2

Abstract

Proteins in the fibrous amyloid state are a major hallmark of neurodegenerative disease. Understanding the multiple conformations, or polymorphs, of amyloid proteins at the molecular level is a challenge of amyloid research. Here, we detail the wide range of polymorphs formed by a segment of human TAR DNA-binding protein 43 (TDP-43) as a model for the polymorphic capabilities of pathological amyloid aggregation. Using X-ray diffraction, microelectron diffraction (MicroED) and single-particle cryo-EM, we show that the 247DLIIKGISVHI 257 segment from the second RNA-recognition motif (RRM2) forms an array of amyloid polymorphs. These associations include seven distinct interfaces displaying five different symmetry classes of steric zippers. Additionally, we find that this segment can adopt three different backbone conformations that contribute to its polymorphic capabilities. In conclusion, the polymorphic nature of this segment illustrates at the molecular level how amyloid proteins can form diverse fibril structures.

Authors:
 [1];  [1]; ORCiD logo [2];  [1];  [1];  [1];  [3];  [1]; ORCiD logo [1]
  1. Univ. of California, Los Angeles, CA (United States)
  2. Wayne State Univ., Detroit, MI (United States); Univ. of California, Los Angeles, CA (United States)
  3. Univ. of California, Los Angeles, CA (United States); Howard Hughes Medical Inst., Ashburn, VA (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
National Inst. of Health; National Science Foundation (NSF)
OSTI Identifier:
1434720
Grant/Contract Number:  
P41 GM103403; NSF MCB 1616265; GM071940; 1S10RR23057; 1U24GM116792; DBI-1338135
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Nature Structural & Molecular Biology
Additional Journal Information:
Journal Volume: 25; Journal Issue: 4; Journal ID: ISSN 1545-9993
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; Cryoelectron microscopy; Peptides; Protein aggregation; RNA-binding proteins; X-ray crystallography

Citation Formats

Guenther, Elizabeth L., Ge, Peng, Trinh, Hamilton, Sawaya, Michael R., Cascio, Duilio, Boyer, David R., Gonen, Tamir, Zhou, Z. Hong, and Eisenberg, David S. Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2. United States: N. p., 2018. Web. doi:10.1038/s41594-018-0045-5.
Guenther, Elizabeth L., Ge, Peng, Trinh, Hamilton, Sawaya, Michael R., Cascio, Duilio, Boyer, David R., Gonen, Tamir, Zhou, Z. Hong, & Eisenberg, David S. Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2. United States. doi:10.1038/s41594-018-0045-5.
Guenther, Elizabeth L., Ge, Peng, Trinh, Hamilton, Sawaya, Michael R., Cascio, Duilio, Boyer, David R., Gonen, Tamir, Zhou, Z. Hong, and Eisenberg, David S. Mon . "Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2". United States. doi:10.1038/s41594-018-0045-5. https://www.osti.gov/servlets/purl/1434720.
@article{osti_1434720,
title = {Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2},
author = {Guenther, Elizabeth L. and Ge, Peng and Trinh, Hamilton and Sawaya, Michael R. and Cascio, Duilio and Boyer, David R. and Gonen, Tamir and Zhou, Z. Hong and Eisenberg, David S.},
abstractNote = {Proteins in the fibrous amyloid state are a major hallmark of neurodegenerative disease. Understanding the multiple conformations, or polymorphs, of amyloid proteins at the molecular level is a challenge of amyloid research. Here, we detail the wide range of polymorphs formed by a segment of human TAR DNA-binding protein 43 (TDP-43) as a model for the polymorphic capabilities of pathological amyloid aggregation. Using X-ray diffraction, microelectron diffraction (MicroED) and single-particle cryo-EM, we show that the 247DLIIKGISVHI257 segment from the second RNA-recognition motif (RRM2) forms an array of amyloid polymorphs. These associations include seven distinct interfaces displaying five different symmetry classes of steric zippers. Additionally, we find that this segment can adopt three different backbone conformations that contribute to its polymorphic capabilities. In conclusion, the polymorphic nature of this segment illustrates at the molecular level how amyloid proteins can form diverse fibril structures.},
doi = {10.1038/s41594-018-0045-5},
journal = {Nature Structural & Molecular Biology},
issn = {1545-9993},
number = 4,
volume = 25,
place = {United States},
year = {2018},
month = {3}
}

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Cited by: 29 works
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