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Design of a new [PSI+]-no-more mutation in SUP35 with strong inhibitory effect on the [PSI+] prion propagation. / Danilov, Lavrentii G.; Matveenko, Andrew G.; Ryzhkova, Varvara E.; Belousov, Mikhail V.; Poleshuk, Olga I.; Likholetova, Daria V.; Sokolov, Petr A.; Kasyanenko, Nina A.; Kajava, Andrey V.; Zhouravleva, Galina A.; Bondarev, Stanislav A.

In: Frontiers in Molecular Neuroscience, Vol. 12, 274, 19.11.2019.

Research output: Contribution to journal › Article › peer-review

Harvard

Danilov, LG, Matveenko, AG, Ryzhkova, VE, Belousov, MV, Poleshuk, OI, Likholetova, DV, Sokolov, PA, Kasyanenko, NA, Kajava, AV, Zhouravleva, GA & Bondarev, SA 2019, 'Design of a new [PSI+]-no-more mutation in SUP35 with strong inhibitory effect on the [PSI+] prion propagation', Frontiers in Molecular Neuroscience, vol. 12, 274. https://doi.org/10.3389/fnmol.2019.00274

APA

Danilov, L. G., Matveenko, A. G., Ryzhkova, V. E., Belousov, M. V., Poleshuk, O. I., Likholetova, D. V., Sokolov, P. A., Kasyanenko, N. A., Kajava, A. V., Zhouravleva, G. A., & Bondarev, S. A. (2019). Design of a new [PSI+]-no-more mutation in SUP35 with strong inhibitory effect on the [PSI+] prion propagation. Frontiers in Molecular Neuroscience, 12, [274]. https://doi.org/10.3389/fnmol.2019.00274

Vancouver

Danilov LG, Matveenko AG, Ryzhkova VE, Belousov MV, Poleshuk OI, Likholetova DV et al. Design of a new [PSI+]-no-more mutation in SUP35 with strong inhibitory effect on the [PSI+] prion propagation. Frontiers in Molecular Neuroscience. 2019 Nov 19;12. 274. https://doi.org/10.3389/fnmol.2019.00274

Author

Danilov, Lavrentii G. ; Matveenko, Andrew G. ; Ryzhkova, Varvara E. ; Belousov, Mikhail V. ; Poleshuk, Olga I. ; Likholetova, Daria V. ; Sokolov, Petr A. ; Kasyanenko, Nina A. ; Kajava, Andrey V. ; Zhouravleva, Galina A. ; Bondarev, Stanislav A. / Design of a new [PSI+]-no-more mutation in SUP35 with strong inhibitory effect on the [PSI+] prion propagation. In: Frontiers in Molecular Neuroscience. 2019 ; Vol. 12.

BibTeX

@article{27ccca351d764e25a9287d6d032bec5d,
title = "Design of a new [PSI+]-no-more mutation in SUP35 with strong inhibitory effect on the [PSI+] prion propagation",
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 vitro and 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.",
keywords = "Amyloid, ArchCandy, Prion, Saccharomyces cerevisiae, SUP35 mutation, superpleated-β-structure, amyloid, prion, [PSI ], [PSI + ], PROTEIN, [PSI+], IDENTIFICATION, TRANSLATION, SACCHAROMYCES-CEREVISIAE, DOMINANT-NEGATIVE INHIBITION, YEAST, GENE, superpleated-beta-structure, DE-NOVO APPEARANCE, REPEATS, DETERMINANT PSI(+)",
author = "Danilov, {Lavrentii G.} and Matveenko, {Andrew G.} and Ryzhkova, {Varvara E.} and Belousov, {Mikhail V.} and Poleshuk, {Olga I.} and Likholetova, {Daria V.} and Sokolov, {Petr A.} and Kasyanenko, {Nina A.} and Kajava, {Andrey V.} and Zhouravleva, {Galina A.} and Bondarev, {Stanislav A.}",
note = "Funding Information: We are grateful to Yury O. Chernoff and Ivana Malcova for plasmids and strains. We thank Ksenia V. Sukhanova, Anton B. Matiiv, Yury A. Barbitoff and Ekaterina Davydova for critical reading of the manuscript and suggestions. The work was supported by the RRC MCT SPbSU and we thank Maxim Vorobyov, Nikolai Kostin and Alexei Masharskiy from this facility for help with experiments. Funding. The authors acknowledge St. Petersburg State University for the research grant (id: 28229898, SB, the ArchCandy analysis). This work was also supported by RFBR grants (19-04-00173, GZ, the analysis of sup35-M0 effects on [PSI +] propagation; 17-54-150002, GZ, and PRC CNRS grant PRC1524, AK, the in vitro experiments; 18-34-00536, AM, the analysis of colocalization of Sup35NM-M0 with the wild-type protein in vivo) and RSF grant (18-14-00050, GZ, the analysis of sup35-M0 effect on the translation termination).",
year = "2019",
month = nov,
day = "19",
doi = "10.3389/fnmol.2019.00274",
language = "English",
volume = "12",
journal = "Frontiers in Molecular Neuroscience",
issn = "1662-5099",
publisher = "Frontiers Media S.A.",

}

RIS

TY - JOUR

T1 - Design of a new [PSI+]-no-more mutation in SUP35 with strong inhibitory effect on the [PSI+] prion propagation

AU - Danilov, Lavrentii G.

AU - Matveenko, Andrew G.

AU - Ryzhkova, Varvara E.

AU - Belousov, Mikhail V.

AU - Poleshuk, Olga I.

AU - Likholetova, Daria V.

AU - Sokolov, Petr A.

AU - Kasyanenko, Nina A.

AU - Kajava, Andrey V.

AU - Zhouravleva, Galina A.

AU - Bondarev, Stanislav A.

N1 - Funding Information: We are grateful to Yury O. Chernoff and Ivana Malcova for plasmids and strains. We thank Ksenia V. Sukhanova, Anton B. Matiiv, Yury A. Barbitoff and Ekaterina Davydova for critical reading of the manuscript and suggestions. The work was supported by the RRC MCT SPbSU and we thank Maxim Vorobyov, Nikolai Kostin and Alexei Masharskiy from this facility for help with experiments. Funding. The authors acknowledge St. Petersburg State University for the research grant (id: 28229898, SB, the ArchCandy analysis). This work was also supported by RFBR grants (19-04-00173, GZ, the analysis of sup35-M0 effects on [PSI +] propagation; 17-54-150002, GZ, and PRC CNRS grant PRC1524, AK, the in vitro experiments; 18-34-00536, AM, the analysis of colocalization of Sup35NM-M0 with the wild-type protein in vivo) and RSF grant (18-14-00050, GZ, the analysis of sup35-M0 effect on the translation termination).

PY - 2019/11/19

Y1 - 2019/11/19

N2 - 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 vitro and 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.

AB - 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 vitro and 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.

KW - Amyloid

KW - ArchCandy

KW - Prion

KW - Saccharomyces cerevisiae

KW - SUP35 mutation

KW - superpleated-β-structure

KW - amyloid

KW - prion

KW - [PSI ]

KW - [PSI + ]

KW - PROTEIN

KW - [PSI+]

KW - IDENTIFICATION

KW - TRANSLATION

KW - SACCHAROMYCES-CEREVISIAE

KW - DOMINANT-NEGATIVE INHIBITION

KW - YEAST

KW - GENE

KW - superpleated-beta-structure

KW - DE-NOVO APPEARANCE

KW - REPEATS

KW - DETERMINANT PSI(+)

UR - http://www.scopus.com/inward/record.url?scp=85076696186&partnerID=8YFLogxK

UR - http://www.mendeley.com/research/design-new-psinomore-mutation-sup35-strong-inhibitory-effect-psi-prion-propagation

U2 - 10.3389/fnmol.2019.00274

DO - 10.3389/fnmol.2019.00274

M3 - Article

VL - 12

JO - Frontiers in Molecular Neuroscience

JF - Frontiers in Molecular Neuroscience

SN - 1662-5099

M1 - 274

ER -

ID: 47747822