NDLI: The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products

Content Provider	PubMed Central
Author	Ripaud, Leslie Maillet, Laurent Cullin, Christophe
Copyright Year	2003
Abstract	The yeast prion [URE3] is a self-propagating inactive form (the propagon) of the Ure2 protein. Ure2p is composed of two domains: residues 1–93—the prion-forming domain (PFD)—and the remaining C-terminal part of the protein, which forms the functional domain involved in nitrogen catabolite repression. Guanidine hydrochloride, and the overproduction of Ure2p 1–65 or Ure2–GFP have been shown to induce the elimination of [URE3]. We demonstrate here, two different curing mechanisms: the inhibition of [URE3] replication by guanidine hydrochloride and its destruction by Ure2p aggregation. Such aggregation is observed if PFD or Ure2–GFP are overproduced and in heterozygous URE2/URE2–GFP, [URE3] diploids. We found that the GFP foci associated with the presence of the prion were dead-end products, the propagons remaining soluble. Surprisingly, [URE3] propagated via the Ure2–GFP fusion protein alone is resistant to these two curing mechanisms and cannot promote the formation of foci. The relationship between aggregation, prion and Hsp104 gives rise to a model in which the propagon is in equilibrium with larger aggregates and functional protein.
Related Links	http://dx.doi.org/10.1093/emboj/cdg488
Ending Page	5259
Page Count	9
Starting Page	5251
File Format	PDF
ISSN	14602075
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	19
Volume Number	22
Language	English
Publisher	Oxford University Press
Publisher Date	2003-10-01
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products

Prion generation in vitro: amyloid of Ure2p is infectious

Curing of the [URE3] prion by Btn2p, a Batten disease-related protein

The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele

The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro

Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells

The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments

Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling

Strains of [PSI+ ] are distinguished by their efficiencies of prion-mediated conformational conversion

The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products

Similar Documents

The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products

Prion generation in vitro: amyloid of Ure2p is infectious

Curing of the [URE3] prion by Btn2p, a Batten disease-related protein

The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele

The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro

Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells

The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments

Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling

Strains of [PSI+ ] are distinguished by their efficiencies of prion-mediated conformational conversion

The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products