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Fibrillogenesis of apomyoglobin facilitated by aggregation sequence of yeast Sup35 in various regions
- Source :
- FEBS Letters. (6):1503-1508
- Publisher :
- Federation of European Biochemical Societies. Published by Elsevier B.V.
-
Abstract
- To examine the effect of aggregation sequence QGGYQQQYNP from yeast Sup35 on fibril formation of sperm whale apomyoglobin (apoMb), we constructed several mutants via substitution. Urea-induced unfolding of apoMb confirms that the substitution of the aggregation sequence does not significantly affect the stability of the mutants compared to wild type (WT) at pH 4.2. Under this condition, however, despite the difference in rate most apoMb mutants form fibrils more readily than WT with distinct morphology. These results suggest that the aggregation sequence facilitates fibril assembly of apoMb at acidic pH in vitro and this facilitation depends on the regions replaced.
- Subjects :
- Male
Models, Molecular
Circular dichroism
Protein Denaturation
Saccharomyces cerevisiae Proteins
Prions
Recombinant Fusion Proteins
Mutant
Molecular Sequence Data
Biophysics
Apomyoglobin
Fibril formation
Sequence (biology)
Saccharomyces cerevisiae
macromolecular substances
Fibril
Biochemistry
Aggregation sequence
Sup35
Structural Biology
Genetics
Animals
Urea
Amino Acid Sequence
Benzothiazoles
Molecular Biology
Chemistry
Myoglobin
Wild type
Whales
Fibrillogenesis
Cell Biology
Hydrogen-Ion Concentration
Yeast
In vitro
Protein Structure, Tertiary
Microscopy, Electron
Thiazoles
Mutation
Apoproteins
Stability
Peptide Termination Factors
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....4b337b0b72bb635470140289d810964e
- Full Text :
- https://doi.org/10.1016/j.febslet.2005.01.059