Linked Life Data

21076138

Source:http://linkedlifedata.com/resource/pubmed/id/21076138

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2010-12-14
pubmed:abstractText
Prions are proteins that can undergo a heritable conformational change to an aggregated amyloid-like state, which is then transmitted to other similar molecules. Ure2, the nitrogen metabolism regulation factor of Saccharomyces cerevisiae, shows prion properties in vivo and forms amyloid fibrils in vitro. Ure2 consists of an N-terminal prion-inducing domain and a C-terminal functional domain. Previous studies have shown that mutations affecting the prion properties of Ure2 are not restricted to the N-terminal prion domain: the deletion of residues 151-158 in the C-domain increases the in vivo prion-inducing propensity of Ure2. Here, we characterized this mutant in vitro and found that the 151-158 deletion has minimal effect on the thermodynamic stability or folding properties of the protein. However, deletion of residues 151-158 accelerates the nucleation, growth and fragmentation of amyloid-like aggregates in vitro, and the aggregates formed are able to seed formation of fibrils of the wild-type protein. In addition, the absence of 151-158 was found to disrupt the inhibitory effect of the Hsp40 chaperone Ydj1 on Ure2 fibril formation. These results suggest that the enhanced in vivo prion-inducing ability of the 151-158 deletion mutant is due to its enhanced ability to generate prion seeds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1741-0134
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-78
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Deletion of a Ure2 C-terminal prion-inhibiting region promotes the rate of fibril seed formation and alters interaction with Hsp40.
pubmed:affiliation
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't