Document Detail


Effects of randomizing the Sup35NM prion domain sequence on formation of amyloid fibrils in vitro.
MedLine Citation:
PMID:  17166483     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The mechanism by which proteins aggregate and form amyloid fibrils is still elusive. In order to preclude interference by cellular factors and to clarify the role of the primary sequence of Sup35p prion domain in formation of amyloid fibrils, we generated five Sup35NM variants by randomizing amino acid sequences in PrDs without altering the amino acid composition and analyzed the in vitro process of amyloid fibril formation. The results showed that each of the five Sup35NM variants polymerized into amyloid fibrils in vitro under native conditions. Furthermore, the Sup35NM variants showed differences in their aggregation time courses. These findings indicate that specific amino acid sequence features in PrD can modify the rate of conversion of Sup35p into amyloid fibrils in vitro.
Authors:
Yingxia Liu; Haiyan Wei; Jianwei Wang; Jianguo Qu; Weiming Zhao; Hung Tao
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-12-06
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  353     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2007 Feb 
Date Detail:
Created Date:  2006-12-25     Completed Date:  2007-02-06     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  139-46     Citation Subset:  IM    
Affiliation:
Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, Peking Union Medical College, Beijing 100005, China.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amyloid / chemistry*,  ultrastructure*
Binding Sites
Dimerization
Fungal Proteins / chemistry*,  ultrastructure
Molecular Sequence Data
Mutagenesis, Site-Directed
Peptide Termination Factors
Prions / chemistry*,  ultrastructure
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Random Allocation
Saccharomyces cerevisiae Proteins / chemistry*,  ultrastructure
Structure-Activity Relationship
Chemical
Reg. No./Substance:
0/Amyloid; 0/Fungal Proteins; 0/Peptide Termination Factors; 0/Prions; 0/SUP35 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins

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