Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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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.
KW - Amyloid/chemistry
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
UR - https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0191317
U2 - 10.1371/journal.pone.0191317
DO - 10.1371/journal.pone.0191317
M3 - Article
C2 - 29381728
VL - 13
SP - e0191317
JO - PLoS ONE
JF - PLoS ONE
SN - 1932-6203
IS - 1
M1 - e0191317
ER -
ID: 13943619