title: Amyloidogenic properties of transthyretin-like protein (TLP) from Escherichia coli.
abstract: We report the amyloid-like properties of Escherichia coli transthyretin-like protein (TLP). TLP is 32% homologous to human transthyretin (hTTR), and is also tetrameric. In contrast to hTTR, TLP does not bind thyroxine. TLP orthologues are found in several prokaryotes, lower eukaryotes and vertebrates. TLP carries a signal peptide that targets the protein to the periplasmic space. We found that TLP and hTTR tetramers dissociate into monomers under similar conditions, although TLP monomers have different association properties. Like hTTR, TLP forms aggregates, small fibrillar structures of 8 nm width, and annular structures of 8 nm diameter which present amyloid-like properties and are toxic to cells.
authors.affiliation: Molecular Neurobiology Unit, Institute for Molecular and Cell Biology, Rua do Campo Alegre 823, Porto, Portugal.
authors.forename: Sofia Duque
authors.initials: SD
authors.lastname: Santos
authors.forename: Rita
authors.initials: R
authors.lastname: Costa
authors.forename: Pedro Filipe
authors.initials: PF
authors.lastname: Teixeira
authors.forename: Max
authors.initials: M
authors.lastname: Gottesman
authors.forename: Isabel
authors.initials: I
authors.lastname: Cardoso
authors.forename: Maria João
authors.initials: MJ
authors.lastname: Saraiva
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000633:toxicity; D045744:Cell Line, Tumor; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000633:toxicity; D019143:Evolution, Molecular; D006801:Humans; D009447:Neuroblastoma; D011228:Prealbumin / Q000737:chemistry* / Q000235:genetics / Q000633:toxicity; D013974:Thyroxine / Q000737:chemistry
chemical_list: D000682:Amyloid; D029968:Escherichia coli Proteins; D011228:Prealbumin; D013974:Thyroxine