Prion properties of the Sup35 protein of yeast Pichia methanolica
Autor: | Vitaly V. Kushnirov, Michael D. Ter-Avanesyan, Natalia V. Kochneva-Pervukhova, Natalia S. Frolova, Maria B. Chechenova |
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Rok vydání: | 2000 |
Předmět: |
Saccharomyces cerevisiae Proteins
Protein family Prions Recombinant Fusion Proteins Molecular Sequence Data Saccharomyces cerevisiae Mitosis Sequence alignment Pichia methanolica Pichia General Biochemistry Genetics and Molecular Biology Conserved sequence Fungal Proteins Suppression Genetic Gene Expression Regulation Fungal Amino Acid Sequence Molecular Biology Crosses Genetic Heat-Shock Proteins Fungal protein Ploidies General Immunology and Microbiology biology General Neuroscience Articles biology.organism_classification Fungal prion Microscopy Fluorescence Biochemistry Endopeptidase K Sequence Alignment Peptide Termination Factors |
Zdroj: | The EMBO Journal. 19:324-331 |
ISSN: | 1460-2075 |
DOI: | 10.1093/emboj/19.3.324 |
Popis: | The Sup35 protein (Sup35p) of Saccharomyces cerevisiae is a translation termination factor of the eRF3 family. The proteins of this family possess a conservative C-terminal domain responsible for translation termination and N-terminal extensions of different structure. The N-terminal domain of Sup35p defines its ability to undergo a heritable prion-like conformational switch, which is manifested as the cytoplasmically inherited [PSI(+)] determinant. Here, we replaced the N-terminal domain of S.cerevisiae Sup35p with an analogous domain from Pichia methanolica. Overexpression of hybrid Sup35p induced the de novo appearance of cytoplasmically inherited suppressor determinants manifesting key genetic and biochemical traits of [PSI(+)]. In contrast to the conventional [PSI(+)], 'hybrid' [PSI(+)] showed lower mitotic stability and preserved their suppressor phenotype upon overexpression of the Hsp104 chaperone protein. The lack of Hsp104 eliminated both types of [PSI(+)]. No transfer of prion state between the two Sup35p variants was observed, which reveals a 'species barrier' for the [PSI(+)] prions. The data obtained show that prion properties are conserved within at least a part of this protein family. |
Databáze: | OpenAIRE |
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