The Conformation of the Prion Domain of Sup35p in Isolation and in the Full-Length Protein

被引：35

作者：

Luckgei, Nina ^{[1
]}

Schuetz, Anne K. ^{[2
]}

Bousset, Luc ^{[3
]}

Habenstein, Birgit ^{[1
]}

Sourigues, Yannick ^{[3
]}

Gardiennet, Carole ^{[1
]}

Meier, Beat H. ^{[2
]}

Melki, Ronald ^{[3
]}

Boeckmann, Anja ^{[1
]}

机构：

[1] Univ Lyon 1, CNRS, Inst Biol & Chim Prot, UMR 5086, F-69367 Lyon, France

[2] ETH, CH-8093 Zurich, Switzerland

[3] CNRS, Lab Enzymol & Biochim Struct, UPR 3082, F-91198 Gif Sur Yvette, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 48期

关键词：

fibrils; prions; proteins; solid-state NMR spectroscopy; Sup35p; SACCHAROMYCES-CEREVISIAE; AMYLOID FIBRILS; SECONDARY STRUCTURE; FUNCTIONAL-ANALYSIS; NMR-SPECTROSCOPY; CHEMICAL-SHIFT; YEAST; TRANSLATION; TERMINATION; VARIANTS;

D O I：

10.1002/anie.201304699

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The whole is not the sum of the parts: Fibrils form both from the full-length Sup35 prion protein and also from its isolated NM domain. A conformation analysis of both shows that Sup35NM and fragments thereof, which are often used as convenient models for prion fibril assembly, have a very different conformation of the prion domains. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：12741 / 12744

页数：4

共 50 条

[41] Stoichiometry and Affinity of Thioflavin T Binding to Sup35p Amyloid Fibrils
Sulatskaya, Anna I.
Kuznetsova, Irina M.
Belousov, Mikhail V.
Bondarev, Stanislav A.
Zhouravleva, Galina A.
Turoverov, Konstantin K.
PLOS ONE, 2016, 11 (05):
[42] Effect of Amino Acid Sequence Rearrangment on Prion Aggregation: Molecular Dynamics Simulations of an Amyloid-forming peptide from the Yeast Prion Sup35p
Song, Youtao
Ji, Yanyan
Zhang, Mengyuan
Yu, Yuanyuan
Yu, Yuan
Li, Hui
He, Jianwei
ISBE 2011: 2011 INTERNATIONAL CONFERENCE ON BIOMEDICINE AND ENGINEERING, VOL 4, 2011, : 113 - 116
[43] Deconvoluting the Cu2+ binding modes of full-length prion protein
Klewpatinond, Mark
Davies, Paul
Bowen, Suzanne
Brown, David R.
Viles, John H.
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (04) : 1870 - 1881
[44] Interdomain interactions of the full-length prion protein studied by molecular dynamics simulations
Mamchur, A.
Panina, I.
Yaroshevich, I.
Kudryavtseva, S.
Stanishneva-Konovalova, T.
FEBS OPEN BIO, 2021, 11 : 355 - 355
[45] Nanoscale insights into full-length prion protein aggregation on model lipid membranes
Pan, Yangang
Wang, Bin
Zhang, Tong
Zhang, Yanan
Wang, Hongda
Xu, Bingqian
CHEMICAL COMMUNICATIONS, 2016, 52 (55) : 8533 - 8536
[46] Effect of metal ions on de novo aggregation of full-length prion protein
Giese, A
Levin, J
Bertsch, U
Kretzschmar, H
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2004, 320 (04) : 1240 - 1246
[47] Solution conformation and heparin-induced dimerization of the full-length extracellular domain of the human amyloid precursor protein
Gralle, M
Oliveira, CLP
Guerreiro, LH
McKinstry, WJ
Galatis, D
Masters, CL
Cappai, R
Parker, MW
Ramos, CHI
Torriani, I
Ferreira, ST
JOURNAL OF MOLECULAR BIOLOGY, 2006, 357 (02) : 493 - 508
[48] Unexpected decrease of full-length prion protein in macaques inoculated with prion-contaminated blood products
Jaffre, Nina
Delmotte, Jerome
Mikol, Jacqueline
Deslys, Jean-Philippe
Comoy, Emmanuel
FRONTIERS IN MOLECULAR BIOSCIENCES, 2023, 10
[49] Comparative analysis of yeast prion strains formed by Sup35 protein derivatives with various deletions in prion domain
Kulichikhin, K. Yu.
Sopova, J. V.
Chernoff, Y. O.
Rubel, A. A.
PRION, 2024, 18 : 3 - 3
[50] Channel Activities of the Full-Length Prion and Truncated Proteins
Wu, Jinming
Wang, Xue
Lakkaraju, Asvin
Sternke-Hoffmann, Rebecca
Qureshi, Bilal M.
Aguzzi, Adriano
Luo, Jinghui
ACS CHEMICAL NEUROSCIENCE, 2023, 15 (01): : 98 - 107

← 1 2 3 4 5 →