Article
Effect of charged residues in the N-domain of Sup35 protein on prion [PSI+] stability and propagation.
The Journal of biological chemistry - 4 Oct 2013
Bondarev Stanislav A, Shchepachev Vadim V, Kajava Andrey V, Zhouravleva Galina A
Abstract excerpt
Recent studies have shown that Sup35p prion fibrils probably have a parallel in-register β-structure. However, the part(s) of the N-domain critical for fibril formation and maintenance of the [PSI(+)] phenotype remains unclear. Here we designed a set of five SUP35 mutant alleles (sup35(KK)) with lysine substitutions in each of five N-domain repeats, and investigated their effect on infectivity and ability of...
Topics
- Alleles
- Amino Acid Sequence
- Amino Acids
- Homozygote
- Kinetics
- Models, Biological
- Molecular Sequence Data
- Mutant Proteins
- Mutation
- Peptide Termination Factors
- Phenotype