Amyloid nucleation and hierarchical assembly of Ure2p fibrils - Role of asparagine/glutamine repeat and nonrepeat regions of the prion domain
文献类型：期刊论文
| 作者 | Jiang, Y ; Li, H ; Zhu, L ; Zhou, JM ; Perrett, S |
| 刊名 | JOURNAL OF BIOLOGICAL CHEMISTRY
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| 出版日期 | 2004 |
| 卷号 | 279期号:5页码:3361 |
| 关键词 | ATOMIC-FORCE MICROSCOPY SACCHAROMYCES-CEREVISIAE IN-VITRO ALZHEIMERS-DISEASE NEURODEGENERATIVE DISEASES PROTEIN DETERMINANT GLUTAMINE REPEATS THIOFLAVINE-T YEAST URE2P AGGREGATION |
| ISSN号 | 0021-9258 |
| 通讯作者 | Zhou, JM: Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, 15 Datun Rd,Chaoyang Dist, Beijing 100101, Peoples R China. |
| 中文摘要 | The yeast prion protein Ure2 forms amyloid-like filaments in vivo and in vitro. This ability depends on the N-terminal prion domain, which contains Asn/Gln repeats, a motif thought to cause human disease by forming stable protein aggregates. The Asn/Gln region of the Ure2p prion domain extends to residue 89, but residues 15-42 represent an island of "normal" random sequence, which is highly conserved in related species and is relatively hydrophobic. We compare the time course of structural changes monitored by thioflavin T (ThT) binding fluorescence and atomic force microscopy for Ure2 and a series of prion domain mutants under a range of conditions. Atomic force microscopy height images at successive time points during a single growth experiment showed the sequential appearance of at least four fibril types that could be readily differentiated by height (5, 8, 12, or 9 nm), morphology (twisted or smooth), and/or time of appearance (early or late in the plateau phase of ThT binding). The Ure2 dimer (h=2.6+/-0.5 nm) and granular particles corresponding to higher order oligomers (h=4-12 nm) could also be detected. The mutants 15Ure2 and Delta15-42Ure2 showed the same time-dependent variation in fibril types but with an increased lag time detected by ThT binding compared with wild-type Ure2. In addition, Delta15-42Ure2 showed reduced binding to ThT. The results imply a role of the conserved region in both amyloid nucleation and formation of the binding surface recognized by ThT. Further, Ure2 amyloid formation is a multistep process via a series of fibrillar intermediates. |
| 收录类别 | SCI |
| 语种 | 英语 |
| 公开日期 | 2013-09-17 |
| 源URL | [http://ir.iphy.ac.cn/handle/311004/33605]  |
| 专题 | 物理研究所_物理所公开发表论文_物理所公开发表论文_期刊论文 |
| 推荐引用方式 GB/T 7714 | Jiang, Y,Li, H,Zhu, L,et al. Amyloid nucleation and hierarchical assembly of Ure2p fibrils - Role of asparagine/glutamine repeat and nonrepeat regions of the prion domain[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2004,279(5):3361. |
| APA | Jiang, Y,Li, H,Zhu, L,Zhou, JM,&Perrett, S.(2004).Amyloid nucleation and hierarchical assembly of Ure2p fibrils - Role of asparagine/glutamine repeat and nonrepeat regions of the prion domain.JOURNAL OF BIOLOGICAL CHEMISTRY,279(5),3361. |
| MLA | Jiang, Y,et al."Amyloid nucleation and hierarchical assembly of Ure2p fibrils - Role of asparagine/glutamine repeat and nonrepeat regions of the prion domain".JOURNAL OF BIOLOGICAL CHEMISTRY 279.5(2004):3361. |
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来源：物理研究所
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