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

• DOI: 10.1371/journal.pone.0191317
• Publication Date: 2018-01-30T18:41:10Z
• Authors: Mikhail V. Belousov; Stanislav A. Bond...; Anastasiia O. Kos...; Kirill S. Antonets; Anna I. Sulatskaya; Maksim I. Sulatsky; Galina A. Zhourav...; Irina M. Kuznetsova; Konstantin K. Tur...; Anton A. Nizhnikov
• Keywords: Amyloid (mycology); Proteome

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