Structural Similarity between the Prion Domain of HET-s and a Homologue Can Explain Amyloid Cross-Seeding in Spite of Limited Sequence Identity

被引：43

作者：

Wasmer, Christian ^{[1
]}

Zimmer, Agnes ^{[2
]}

Sabate, Raimon ^{[3
]}

Soragni, Alice ^{[1
]}

Saupe, Sven J. ^{[3
]}

Ritter, Christiane ^{[2
]}

Meier, Beat H. ^{[1
]}

机构：

[1] ETH, CH-8093 Zurich, Switzerland

[2] Helmholtz Ctr Infect Res, D-38124 Braunschweig, Germany

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

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2010年 / 402卷 / 02期

关键词：

prion; amyloid; fibrils; HET-s protein; FgHET-s protein; SOLID-STATE NMR; RESONANCE ASSIGNMENT; HET-S(218-289) PRION; PROTEIN-STRUCTURE; ALPHA; C-13; POLARIZATION; FIBRILS; ENHANCEMENT; STABILITY;

D O I：

10.1016/j.jmb.2010.06.053

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We describe a distant homologue of the fungal HET-s prion, which is found in the fungus Fusarium graminearum. The domain FgHET-s(218-289), which corresponds to the prion domain in HET-s from Podospora anserina, forms amyloid fibrils in vitro and is able to efficiently cross-seed HET-s(218-289) prion formation. We structurally characterize FgHET-s(218-289), which displays 38% sequence identity with HET-s(218-289). Solid-state NMR and hydrogen/deuterium exchange detected by NMR show that the fold and a number of structural details are very similar for the prion domains of the two proteins. This structural similarity readily explains why cross-seeding occurs here in spite of the sequence divergence. (C) 2010 Elsevier Ltd. All rights reserved.

引用

收藏

页码：311 / 325

页数：15

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