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	Hsp40 interacts directly with the native state of the yeast prion protein ure2 and inhibits formation of amyloid-like fibrils
	Lian, Hui-Yong; Zhang, Hong; Zhang, Zai-Rong; Loovers, Harriet M.; Jones, Gary W.; Rowling, Pamela J. E.; Itzhaki, Laura S.; Zhou, Jun-Mei; Perrett, Sarah
刊名	Journal of biological chemistry
	2007-04-20
卷号	282期号:16页码:11931-11940
ISSN号	0021-9258
DOI	10.1074/jbc.m606856200
通讯作者	Perrett, sarah(sarah.perrett@iname.com)
英文摘要	Ure2 is the protein determinant of the [ ure3] prion phenotype in saccharomyces cerevisiae and consists of a flexible n-terminal prion-determining domain and a globular c-terminal glutathione transferase-like domain. overexpression of the type i hsp40 member ydj1 in yeast cells has been found to result in the loss of [ ure3]. however, the mechanism of prion curing by ydj1 remains unclear. here we tested the effect of overexpression of hsp40 members ydj1, sis1, and apj1 and also hsp70 co-chaperones cpr7, cns1, sti1, and fes1 in vivo and found that only ydj1 showed a strong curing effect on [ ure3]. we also investigated the interaction of ydj1 with ure2 in vitro. we found that ydj1 was able to suppress formation of amyloid-like fibrils of ure2 by delaying the process of fibril formation, as monitored by thioflavin t binding and atomic force microscopy imaging. controls using bovine serum albumin, sis1, or the human hsp40 homologues hdj1 or hdj2 showed no significant inhibitory effect. ydj1 was only effective when added during the lag phase of fibril formation, suggesting that it interacts with ure2 at an early stage in fibril formation and delays the nucleation process. using surface plasmon resonance and size exclusion chromatography, we demonstrated a direct interaction between ydj1 and both wild type and n-terminally truncated ure2. in contrast, hdj2, which did not suppress fibril formation, did not show this interaction. the results suggest that ydj1 inhibits ure2 fibril formation by binding to the native state of ure2, thus delaying the onset of oligomerization.
WOS关键词	SACCHAROMYCES-CEREVISIAE ; MOLECULAR CHAPERONES ; DNAJ HOMOLOG ; IN-VITRO ; ATPASE ACTIVITY ; HSP70 ; DOMAIN ; PROPAGATION ; AGGREGATION ; GLUTATHIONE
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
语种	英语
出版者	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
WOS记录号	WOS:000245941900036
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2380490
专题	中国科学院大学
通讯作者	Perrett, Sarah
作者单位	1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Natl Univ Ireland Maynooth, Dept Biol, Maynooth, Kildare, Ireland 3.Hutchison Med Res Council, Res Ctr, Canc Cell Unit, Cambridge CB2 0XZ, England 4.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
推荐引用方式 GB/T 7714	Lian, Hui-Yong,Zhang, Hong,Zhang, Zai-Rong,et al. Hsp40 interacts directly with the native state of the yeast prion protein ure2 and inhibits formation of amyloid-like fibrils[J]. Journal of biological chemistry,2007,282(16):11931-11940.
APA	Lian, Hui-Yong.,Zhang, Hong.,Zhang, Zai-Rong.,Loovers, Harriet M..,Jones, Gary W..,...&Perrett, Sarah.(2007).Hsp40 interacts directly with the native state of the yeast prion protein ure2 and inhibits formation of amyloid-like fibrils.Journal of biological chemistry,282(16),11931-11940.
MLA	Lian, Hui-Yong,et al."Hsp40 interacts directly with the native state of the yeast prion protein ure2 and inhibits formation of amyloid-like fibrils".Journal of biological chemistry 282.16(2007):11931-11940.

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