Solid-State NMR Spectroscopy Reveals that E. coli Inclusion Bodies of HET-s(218-289) are Amyloids

被引：66

作者：

Wasmer, Christian ^{[1
]}

Benkemoun, Laura ^{[2
]}

Sabate, Raimon ^{[2
]}

Steinmetz, Michel O. ^{[3
]}

Coulary-Salin, Benedicte ^{[2
]}

Wang, Lei ^{[1
]}

Riek, Roland ^{[1
]}

Saupe, Sven J. ^{[2
]}

Meier, Beat H. ^{[1
]}

机构：

[1] ETH, Phys Chem Lab, CH-8093 Zurich, Switzerland

[2] Univ Bordeaux 2, CNRS, Lab Genet Mol Champignons, IBGC UMR 5095, F-33076 Bordeaux, France

[3] Paul Scherrer Inst, CH-5232 Villigen, Switzerland

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 26期

基金：

瑞士国家科学基金会;

关键词：

amyloids; inclusion bodies; NMR spectroscopy; proteins; structure elucidation; S PRION PROTEIN; HET-S; ORGANIZATION; PRODUCT; BEHAVES; CORE; GENE;

D O I：

10.1002/anie.200806100

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Protein deposition frequently occurs as inclusion bodies (IBs) during heterologous protein expression in E. coli. The structure of these E. coli IBs of the prion-forming domain from the fungal prion HET-s is the same as that previously determined for fibrils assembled in vitro, and show prion infectivity. These results demonstrate that the IBs of HET-s(218-289) are amyloids. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

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页码：4858 / 4860

页数：3

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