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Modification of [PSI+] prion properties by combining amino acid changes in N-terminal domain of Sup35 protein. / Bondarev, S.A.; Shirokolobova, E.D.; Trubitsina, N.P.; Zhouravleva, G.A.

в: Molecular Biology, № 2, 2014, стр. 270-277.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Bondarev, SA, Shirokolobova, ED, Trubitsina, NP & Zhouravleva, GA 2014, 'Modification of [PSI+] prion properties by combining amino acid changes in N-terminal domain of Sup35 protein', Molecular Biology, № 2, стр. 270-277. https://doi.org/10.1134/S0026893314020034

APA

Bondarev, S. A., Shirokolobova, E. D., Trubitsina, N. P., & Zhouravleva, G. A. (2014). Modification of [PSI+] prion properties by combining amino acid changes in N-terminal domain of Sup35 protein. Molecular Biology, (2), 270-277. https://doi.org/10.1134/S0026893314020034

Vancouver

Bondarev SA, Shirokolobova ED, Trubitsina NP, Zhouravleva GA. Modification of [PSI+] prion properties by combining amino acid changes in N-terminal domain of Sup35 protein. Molecular Biology. 2014;(2):270-277. https://doi.org/10.1134/S0026893314020034

Author

Bondarev, S.A. ; Shirokolobova, E.D. ; Trubitsina, N.P. ; Zhouravleva, G.A. / Modification of [PSI+] prion properties by combining amino acid changes in N-terminal domain of Sup35 protein. в: Molecular Biology. 2014 ; № 2. стр. 270-277.

BibTeX

@article{d94612218da54f22b096796def9b24ab,
title = "Modification of [PSI+] prion properties by combining amino acid changes in N-terminal domain of Sup35 protein",
abstract = "The prion [PSI +] is an amyloid isoform of the release factor eRF3 encoded by the SUP35 gene in Saccharomyces cerevisiae yeast. Naturally occurring amyloid complexes have been studied for a long time, yet their structural organization is still not well understood. The formation of amyloid forms of the wild-type Sup35 protein (Sup35p) is directed by its N-terminal portion, which forms a superpleated β-sheet structure. We previously constructed five mutants, each of which carried a replacement in two consecutive amino acids, one in each of the oligopeptide repeats (OR) and in the Sup35p N-terminal region. Mutations sup35-M1 (YQ46-47KK) and sup35-M2 (QQ61-62KK) lead to the compete loss of prion conformation. Three other mutants, i.e., sup35-M3 (QQ70-71KK), sup35-M4 (QQ80-81KK), and sup35-M5 (QQ89-90KK), formed functional prions. In the current study, we investigated the contribution of each mutant peptide to the stability of the prion and aggregation properties, and compared the effects of single mutants and com",
author = "S.A. Bondarev and E.D. Shirokolobova and N.P. Trubitsina and G.A. Zhouravleva",
year = "2014",
doi = "10.1134/S0026893314020034",
language = "English",
pages = "270--277",
journal = "Molecular Biology",
issn = "0026-8933",
publisher = "Pleiades Publishing",
number = "2",

}

RIS

TY - JOUR

T1 - Modification of [PSI+] prion properties by combining amino acid changes in N-terminal domain of Sup35 protein

AU - Bondarev, S.A.

AU - Shirokolobova, E.D.

AU - Trubitsina, N.P.

AU - Zhouravleva, G.A.

PY - 2014

Y1 - 2014

N2 - The prion [PSI +] is an amyloid isoform of the release factor eRF3 encoded by the SUP35 gene in Saccharomyces cerevisiae yeast. Naturally occurring amyloid complexes have been studied for a long time, yet their structural organization is still not well understood. The formation of amyloid forms of the wild-type Sup35 protein (Sup35p) is directed by its N-terminal portion, which forms a superpleated β-sheet structure. We previously constructed five mutants, each of which carried a replacement in two consecutive amino acids, one in each of the oligopeptide repeats (OR) and in the Sup35p N-terminal region. Mutations sup35-M1 (YQ46-47KK) and sup35-M2 (QQ61-62KK) lead to the compete loss of prion conformation. Three other mutants, i.e., sup35-M3 (QQ70-71KK), sup35-M4 (QQ80-81KK), and sup35-M5 (QQ89-90KK), formed functional prions. In the current study, we investigated the contribution of each mutant peptide to the stability of the prion and aggregation properties, and compared the effects of single mutants and com

AB - The prion [PSI +] is an amyloid isoform of the release factor eRF3 encoded by the SUP35 gene in Saccharomyces cerevisiae yeast. Naturally occurring amyloid complexes have been studied for a long time, yet their structural organization is still not well understood. The formation of amyloid forms of the wild-type Sup35 protein (Sup35p) is directed by its N-terminal portion, which forms a superpleated β-sheet structure. We previously constructed five mutants, each of which carried a replacement in two consecutive amino acids, one in each of the oligopeptide repeats (OR) and in the Sup35p N-terminal region. Mutations sup35-M1 (YQ46-47KK) and sup35-M2 (QQ61-62KK) lead to the compete loss of prion conformation. Three other mutants, i.e., sup35-M3 (QQ70-71KK), sup35-M4 (QQ80-81KK), and sup35-M5 (QQ89-90KK), formed functional prions. In the current study, we investigated the contribution of each mutant peptide to the stability of the prion and aggregation properties, and compared the effects of single mutants and com

U2 - 10.1134/S0026893314020034

DO - 10.1134/S0026893314020034

M3 - Article

SP - 270

EP - 277

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 2

ER -

ID: 7049694