Screening for amyloid proteins in the yeast proteome

Tatyana Ryzhova, Julia V Sopova, Sergey P Zadorsky, Vera A Siniukova, Aleksandra V Sergeeva, Svetlana A Galkina, Anton A Nizhnikov, Aleksandr A Shenfeld, Kirill V Volkov, Alexey P. Galkin

Результат исследований: Научные публикации в периодических изданияхстатьянаучнаярецензирование

5 Цитирования (Scopus)

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The search for novel pathological and functional amyloids represents one of the most important tasks of contemporary biomedicine. Formation of pathological amyloid fibrils in the aging brain causes incurable neurodegenerative disorders such as Alzheimer's, Parkinson's Huntington's diseases. At the same time, a set of amyloids regulates vital processes in archaea, prokaryotes and eukaryotes. Our knowledge of the prevalence and biological significance of amyloids is limited due to the lack of universal methods for their identification. Here, using our original method of proteomic screening PSIA-LC-MALDI, we identified a number of proteins that form amyloid-like detergent-resistant aggregates in Saccharomyces cerevisiae. We revealed in yeast strains of different origin known yeast prions, prion-associated proteins, and a set of proteins whose amyloid properties were not shown before. A substantial number of the identified proteins are cell wall components, suggesting that amyloids may play important roles in the formation of this extracellular protective sheath. Two proteins identified in our screen, Gas1 and Ygp1, involved in biogenesis of the yeast cell wall, were selected for detailed analysis of amyloid properties. We show that Gas1 and Ygp1 demonstrate amyloid properties both in vivo in yeast cells and using the bacteria-based system C-DAG. Taken together, our data show that this proteomic approach is very useful for identification of novel amyloids.

Язык оригиналаанглийский
Страницы (с-по)469-478
Число страниц10
ЖурналCurrent Genetics
Том64
Номер выпуска2
DOI
СостояниеОпубликовано - 2018

Ключевые слова

    Цитировать

    Ryzhova, T., Sopova, J. V., Zadorsky, S. P., Siniukova, V. A., Sergeeva, A. V., Galkina, S. A., ... Galkin, A. P. (2018). Screening for amyloid proteins in the yeast proteome. Current Genetics, 64(2), 469-478. https://doi.org/10.1007/s00294-017-0759-7
    Ryzhova, Tatyana ; Sopova, Julia V ; Zadorsky, Sergey P ; Siniukova, Vera A ; Sergeeva, Aleksandra V ; Galkina, Svetlana A ; Nizhnikov, Anton A ; Shenfeld, Aleksandr A ; Volkov, Kirill V ; Galkin, Alexey P. / Screening for amyloid proteins in the yeast proteome. В: Current Genetics. 2018 ; Том 64, № 2. стр. 469-478.
    @article{3535d294ff9e4b509ef3c861e60a343f,
    title = "Screening for amyloid proteins in the yeast proteome",
    abstract = "The search for novel pathological and functional amyloids represents one of the most important tasks of contemporary biomedicine. Formation of pathological amyloid fibrils in the aging brain causes incurable neurodegenerative disorders such as Alzheimer's, Parkinson's Huntington's diseases. At the same time, a set of amyloids regulates vital processes in archaea, prokaryotes and eukaryotes. Our knowledge of the prevalence and biological significance of amyloids is limited due to the lack of universal methods for their identification. Here, using our original method of proteomic screening PSIA-LC-MALDI, we identified a number of proteins that form amyloid-like detergent-resistant aggregates in Saccharomyces cerevisiae. We revealed in yeast strains of different origin known yeast prions, prion-associated proteins, and a set of proteins whose amyloid properties were not shown before. A substantial number of the identified proteins are cell wall components, suggesting that amyloids may play important roles in the formation of this extracellular protective sheath. Two proteins identified in our screen, Gas1 and Ygp1, involved in biogenesis of the yeast cell wall, were selected for detailed analysis of amyloid properties. We show that Gas1 and Ygp1 demonstrate amyloid properties both in vivo in yeast cells and using the bacteria-based system C-DAG. Taken together, our data show that this proteomic approach is very useful for identification of novel amyloids.",
    keywords = "Alzheimer Disease/genetics, Amyloid/genetics, Amyloidogenic Proteins/genetics, Humans, Prion Proteins/genetics, Prokaryotic Cells/metabolism, Proteome/genetics, Proteomics, Saccharomyces cerevisiae/genetics",
    author = "Tatyana Ryzhova and Sopova, {Julia V} and Zadorsky, {Sergey P} and Siniukova, {Vera A} and Sergeeva, {Aleksandra V} and Galkina, {Svetlana A} and Nizhnikov, {Anton A} and Shenfeld, {Aleksandr A} and Volkov, {Kirill V} and Galkin, {Alexey P.}",
    year = "2018",
    doi = "10.1007/s00294-017-0759-7",
    language = "English",
    volume = "64",
    pages = "469--478",
    journal = "Current Genetics",
    issn = "0172-8083",
    publisher = "Springer",
    number = "2",

    }

    Ryzhova, T, Sopova, JV, Zadorsky, SP, Siniukova, VA, Sergeeva, AV, Galkina, SA, Nizhnikov, AA, Shenfeld, AA, Volkov, KV & Galkin, AP 2018, 'Screening for amyloid proteins in the yeast proteome' Current Genetics, том. 64, № 2, стр. 469-478. https://doi.org/10.1007/s00294-017-0759-7

    Screening for amyloid proteins in the yeast proteome. / Ryzhova, Tatyana; Sopova, Julia V; Zadorsky, Sergey P; Siniukova, Vera A; Sergeeva, Aleksandra V; Galkina, Svetlana A; Nizhnikov, Anton A; Shenfeld, Aleksandr A; Volkov, Kirill V; Galkin, Alexey P.

    В: Current Genetics, Том 64, № 2, 2018, стр. 469-478.

    Результат исследований: Научные публикации в периодических изданияхстатьянаучнаярецензирование

    TY - JOUR

    T1 - Screening for amyloid proteins in the yeast proteome

    AU - Ryzhova, Tatyana

    AU - Sopova, Julia V

    AU - Zadorsky, Sergey P

    AU - Siniukova, Vera A

    AU - Sergeeva, Aleksandra V

    AU - Galkina, Svetlana A

    AU - Nizhnikov, Anton A

    AU - Shenfeld, Aleksandr A

    AU - Volkov, Kirill V

    AU - Galkin, Alexey P.

    PY - 2018

    Y1 - 2018

    N2 - The search for novel pathological and functional amyloids represents one of the most important tasks of contemporary biomedicine. Formation of pathological amyloid fibrils in the aging brain causes incurable neurodegenerative disorders such as Alzheimer's, Parkinson's Huntington's diseases. At the same time, a set of amyloids regulates vital processes in archaea, prokaryotes and eukaryotes. Our knowledge of the prevalence and biological significance of amyloids is limited due to the lack of universal methods for their identification. Here, using our original method of proteomic screening PSIA-LC-MALDI, we identified a number of proteins that form amyloid-like detergent-resistant aggregates in Saccharomyces cerevisiae. We revealed in yeast strains of different origin known yeast prions, prion-associated proteins, and a set of proteins whose amyloid properties were not shown before. A substantial number of the identified proteins are cell wall components, suggesting that amyloids may play important roles in the formation of this extracellular protective sheath. Two proteins identified in our screen, Gas1 and Ygp1, involved in biogenesis of the yeast cell wall, were selected for detailed analysis of amyloid properties. We show that Gas1 and Ygp1 demonstrate amyloid properties both in vivo in yeast cells and using the bacteria-based system C-DAG. Taken together, our data show that this proteomic approach is very useful for identification of novel amyloids.

    AB - The search for novel pathological and functional amyloids represents one of the most important tasks of contemporary biomedicine. Formation of pathological amyloid fibrils in the aging brain causes incurable neurodegenerative disorders such as Alzheimer's, Parkinson's Huntington's diseases. At the same time, a set of amyloids regulates vital processes in archaea, prokaryotes and eukaryotes. Our knowledge of the prevalence and biological significance of amyloids is limited due to the lack of universal methods for their identification. Here, using our original method of proteomic screening PSIA-LC-MALDI, we identified a number of proteins that form amyloid-like detergent-resistant aggregates in Saccharomyces cerevisiae. We revealed in yeast strains of different origin known yeast prions, prion-associated proteins, and a set of proteins whose amyloid properties were not shown before. A substantial number of the identified proteins are cell wall components, suggesting that amyloids may play important roles in the formation of this extracellular protective sheath. Two proteins identified in our screen, Gas1 and Ygp1, involved in biogenesis of the yeast cell wall, were selected for detailed analysis of amyloid properties. We show that Gas1 and Ygp1 demonstrate amyloid properties both in vivo in yeast cells and using the bacteria-based system C-DAG. Taken together, our data show that this proteomic approach is very useful for identification of novel amyloids.

    KW - Alzheimer Disease/genetics

    KW - Amyloid/genetics

    KW - Amyloidogenic Proteins/genetics

    KW - Humans

    KW - Prion Proteins/genetics

    KW - Prokaryotic Cells/metabolism

    KW - Proteome/genetics

    KW - Proteomics

    KW - Saccharomyces cerevisiae/genetics

    U2 - 10.1007/s00294-017-0759-7

    DO - 10.1007/s00294-017-0759-7

    M3 - Article

    VL - 64

    SP - 469

    EP - 478

    JO - Current Genetics

    JF - Current Genetics

    SN - 0172-8083

    IS - 2

    ER -

    Ryzhova T, Sopova JV, Zadorsky SP, Siniukova VA, Sergeeva AV, Galkina SA и соавт. Screening for amyloid proteins in the yeast proteome. Current Genetics. 2018;64(2):469-478. https://doi.org/10.1007/s00294-017-0759-7