M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils

Mikhail V Belousov, Stanislav A Bondarev, Anastasiia O Kosolapova, Kirill S Antonets, Anna I Sulatskaya, Maksim I Sulatsky, Galina A Zhouravleva, Irina M Kuznetsova, Konstantin K Turoverov, Anton A Nizhnikov

Результат исследований: Научные публикации в периодических изданияхстатья

4 Цитирования (Scopus)

Выдержка

Amyloids are protein fibrils with a characteristic spatial structure. Amyloids were long perceived as the pathogens involved in a set of lethal diseases in humans and animals. In recent decades, it has become clear that amyloids represent a quaternary protein structure that is not only pathological but also functionally important and is widely used by different organisms, ranging from archaea to animals, to implement diverse biological functions. The greatest biological variety of amyloids is found in prokaryotes, where they control the formation of biofilms and cell wall sheaths, facilitate the overcoming of surface tension, and regulate the metabolism of toxins. Several amyloid proteins were identified in the important model, biotechnological and pathogenic bacterium Escherichia coli. In previous studies, using a method for the proteomic screening and identification of amyloids, we identified 61 potentially amyloidogenic proteins in the proteome of E. coli. Among these proteins, YghJ was the most enriched with bioinformatically predicted amyloidogenic regions. YghJ is a lipoprotein with a zinc metalloprotease M60-like domain that is involved in mucin degradation in the intestine as well as in proinflammatory responses. In this study, we analyzed the amyloid properties of the YghJ M60-like domain and demonstrated that it forms amyloid-like fibrils in vitro and in vivo.

Язык оригиналаанглийский
Номер статьиe0191317
Страницы (с-по)e0191317
Число страниц17
ЖурналPLoS ONE
Том13
Номер выпуска1
DOI
СостояниеОпубликовано - 2018

Отпечаток

Escherichia coli Proteins
Metalloproteases
metalloproteinases
amyloid
Amyloid
Escherichia coli
Amyloidogenic Proteins
Proteins
proteins
Animals
Quaternary Protein Structure
protein quaternary structure
Biofilms
Mucins
Pathogens
Proteome
Surface Tension
diseases and disorders (animals and humans)
Metabolism
Archaea

Предметные области Scopus

  • Земледелие и биологические науки (все)
  • Биохимия, генетика и молекулярная биология (все)

Цитировать

Belousov, Mikhail V ; Bondarev, Stanislav A ; Kosolapova, Anastasiia O ; Antonets, Kirill S ; Sulatskaya, Anna I ; Sulatsky, Maksim I ; Zhouravleva, Galina A ; Kuznetsova, Irina M ; Turoverov, Konstantin K ; Nizhnikov, Anton A. / M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. В: PLoS ONE. 2018 ; Том 13, № 1. стр. e0191317.
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abstract = "Amyloids are protein fibrils with a characteristic spatial structure. Amyloids were long perceived as the pathogens involved in a set of lethal diseases in humans and animals. In recent decades, it has become clear that amyloids represent a quaternary protein structure that is not only pathological but also functionally important and is widely used by different organisms, ranging from archaea to animals, to implement diverse biological functions. The greatest biological variety of amyloids is found in prokaryotes, where they control the formation of biofilms and cell wall sheaths, facilitate the overcoming of surface tension, and regulate the metabolism of toxins. Several amyloid proteins were identified in the important model, biotechnological and pathogenic bacterium Escherichia coli. In previous studies, using a method for the proteomic screening and identification of amyloids, we identified 61 potentially amyloidogenic proteins in the proteome of E. coli. Among these proteins, YghJ was the most enriched with bioinformatically predicted amyloidogenic regions. YghJ is a lipoprotein with a zinc metalloprotease M60-like domain that is involved in mucin degradation in the intestine as well as in proinflammatory responses. In this study, we analyzed the amyloid properties of the YghJ M60-like domain and demonstrated that it forms amyloid-like fibrils in vitro and in vivo.",
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M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. / Belousov, Mikhail V; Bondarev, Stanislav A; Kosolapova, Anastasiia O; Antonets, Kirill S; Sulatskaya, Anna I; Sulatsky, Maksim I; Zhouravleva, Galina A; Kuznetsova, Irina M; Turoverov, Konstantin K; Nizhnikov, Anton A.

В: PLoS ONE, Том 13, № 1, e0191317, 2018, стр. e0191317.

Результат исследований: Научные публикации в периодических изданияхстатья

TY - JOUR

T1 - M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils

AU - Belousov, Mikhail V

AU - Bondarev, Stanislav A

AU - Kosolapova, Anastasiia O

AU - Antonets, Kirill S

AU - Sulatskaya, Anna I

AU - Sulatsky, Maksim I

AU - Zhouravleva, Galina A

AU - Kuznetsova, Irina M

AU - Turoverov, Konstantin K

AU - Nizhnikov, Anton A

PY - 2018

Y1 - 2018

N2 - Amyloids are protein fibrils with a characteristic spatial structure. Amyloids were long perceived as the pathogens involved in a set of lethal diseases in humans and animals. In recent decades, it has become clear that amyloids represent a quaternary protein structure that is not only pathological but also functionally important and is widely used by different organisms, ranging from archaea to animals, to implement diverse biological functions. The greatest biological variety of amyloids is found in prokaryotes, where they control the formation of biofilms and cell wall sheaths, facilitate the overcoming of surface tension, and regulate the metabolism of toxins. Several amyloid proteins were identified in the important model, biotechnological and pathogenic bacterium Escherichia coli. In previous studies, using a method for the proteomic screening and identification of amyloids, we identified 61 potentially amyloidogenic proteins in the proteome of E. coli. Among these proteins, YghJ was the most enriched with bioinformatically predicted amyloidogenic regions. YghJ is a lipoprotein with a zinc metalloprotease M60-like domain that is involved in mucin degradation in the intestine as well as in proinflammatory responses. In this study, we analyzed the amyloid properties of the YghJ M60-like domain and demonstrated that it forms amyloid-like fibrils in vitro and in vivo.

AB - Amyloids are protein fibrils with a characteristic spatial structure. Amyloids were long perceived as the pathogens involved in a set of lethal diseases in humans and animals. In recent decades, it has become clear that amyloids represent a quaternary protein structure that is not only pathological but also functionally important and is widely used by different organisms, ranging from archaea to animals, to implement diverse biological functions. The greatest biological variety of amyloids is found in prokaryotes, where they control the formation of biofilms and cell wall sheaths, facilitate the overcoming of surface tension, and regulate the metabolism of toxins. Several amyloid proteins were identified in the important model, biotechnological and pathogenic bacterium Escherichia coli. In previous studies, using a method for the proteomic screening and identification of amyloids, we identified 61 potentially amyloidogenic proteins in the proteome of E. coli. Among these proteins, YghJ was the most enriched with bioinformatically predicted amyloidogenic regions. YghJ is a lipoprotein with a zinc metalloprotease M60-like domain that is involved in mucin degradation in the intestine as well as in proinflammatory responses. In this study, we analyzed the amyloid properties of the YghJ M60-like domain and demonstrated that it forms amyloid-like fibrils in vitro and in vivo.

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KW - Escherichia coli Proteins/chemistry

KW - Metalloproteases/chemistry

KW - Protein Domains

KW - Protein Multimerization

KW - Protein Structure, Secondary

KW - SYSTEM

KW - CELLS

KW - BACTERIA

KW - SECRETED METALLOPROTEASE

KW - SEQUENCES

KW - ALGORITHM

KW - FUNCTIONAL AMYLOIDS

KW - PRION

KW - THIOFLAVIN T

KW - HISTORY

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DO - 10.1371/journal.pone.0191317

M3 - Article

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VL - 13

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JF - PLoS ONE

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