M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils.
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...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2018-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC5790219?pdf=render |
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| author | 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 |
| author_facet | 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 |
| author_sort | Mikhail V Belousov |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-21T10:24:21Z |
| format | Article |
| id | doaj.art-003509b91b074657a28c66683c3a6963 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T10:24:21Z |
| publishDate | 2018-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-003509b91b074657a28c66683c3a69632022-12-21T19:07:20ZengPublic Library of Science (PLoS)PLoS ONE1932-62032018-01-01131e019131710.1371/journal.pone.0191317M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils.Mikhail V BelousovStanislav A BondarevAnastasiia O KosolapovaKirill S AntonetsAnna I SulatskayaMaksim I SulatskyGalina A ZhouravlevaIrina M KuznetsovaKonstantin K TuroverovAnton A NizhnikovAmyloids 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.http://europepmc.org/articles/PMC5790219?pdf=render |
| spellingShingle | 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 M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. PLoS ONE |
| title | M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. |
| title_full | M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. |
| title_fullStr | M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. |
| title_full_unstemmed | M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. |
| title_short | M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. |
| title_sort | m60 like metalloprotease domain of the escherichia coli yghj protein forms amyloid fibrils |
| url | http://europepmc.org/articles/PMC5790219?pdf=render |
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