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http://hdl.handle.net/11701/16600
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Поле DC | Значение | Язык |
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dc.contributor.author | Danilov, Lavrentii G | - |
dc.contributor.author | Matveenko, Andrew G | - |
dc.contributor.author | Ryzhkova, Varvara E | - |
dc.contributor.author | Belousov, Mikhail V | - |
dc.contributor.author | Poleshchuk, Olga I | - |
dc.contributor.author | Likholetova, Daria V | - |
dc.contributor.author | Sokolov, Petr A | - |
dc.contributor.author | Kasyanenko, Nina A | - |
dc.contributor.author | Kajava, Andrey V | - |
dc.contributor.author | Zhouravleva, Galina A | - |
dc.contributor.author | Bondarev, Stanislav A | - |
dc.date.accessioned | 2019-11-19T11:23:38Z | - |
dc.date.available | 2019-11-19T11:23:38Z | - |
dc.date.issued | 2019-11-19 | - |
dc.identifier.citation | Danilov et al., 2019 | en_GB |
dc.identifier.other | doi: 10.3389/fnmol.2019.00274 | - |
dc.identifier.uri | http://hdl.handle.net/11701/16600 | - |
dc.description.abstract | A number of [PSI+]-no-more (PNM) mutations, eliminating [PSI+] prion, were previously described in SUP35. In this study, we designed and analyzed a new PNM mutation based on the parallel in-register β-structure of Sup35 prion fibrils suggested by the known experimental data. In such an arrangement, substitution of non-charged residues by charged ones may destabilize the fibril structure. We introduced Q33K/A34K amino acid substitutions into the Sup35 protein, corresponding allele was called sup35-M0. The mutagenized residues were chosen based on ArchCandy in silico prediction of high inhibitory effect on the amyloidogenic potential of Sup35. The experiments confirmed that Sup35-M0 leads to the elimination of [PSI+] with high efficiency. Our data suggested that the elimination of the [PSI+] prion is associated with the decreased aggregation properties of the protein. The new mutation can induce the prion with very low efficiency and is able to propagate only weak [PSI+] prion variants. We also showed that Sup35-M0 protein co-aggregates with the wild-type Sup35 in vivo. Moreover, our data confirmed the utility of the strategy of substitution of non-charged residues by charged ones to design new mutations to inhibit a prion formation | en_GB |
dc.description.sponsorship | RFBR grant 19-04-00173, RFBR grant 17-54-150002, and PRC CNRS grant PRC1524,18-34-00536, RSF grant 18-14-00050 | en_GB |
dc.language.iso | en | en_GB |
dc.publisher | Frontiers in Molecular Neuroscience | en_GB |
dc.relation.ispartofseries | 12;274 | - |
dc.subject | [PSI+], amyloid, ArchCandy, prion, Saccharomyces cerevisiae, SUP35 mutation, superpleated-β-structure | en_GB |
dc.title | Design of a New [PSI+]-No-More Mutation in SUP35 With Strong Inhibitory Effect on the [PSI+] Prion Propagation | en_GB |
dc.title.alternative | New PNM Mutation in SUP35 | en_GB |
dc.type | Article | en_GB |
dc.type | Working Paper | en_GB |
Располагается в коллекциях: | Articles |
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Файл | Описание | Размер | Формат | |
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Danilov_et_al_2019.pdf | 1,53 MB | Adobe PDF | Просмотреть/Открыть |
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