期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 402, 期 2, 页码 311-325出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.06.053
关键词
prion; amyloid; fibrils; HET-s protein; FgHET-s protein
资金
- Eidgenossische Technische Hochschule Zurich
- Centre National de la Recherche Scientifique
- Helmholtz-Gemeinschaft
- TRANS-DEATH EC grant
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.
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