Amyloidogenic properties of transthyretin-like protein (TLP) from Escherichia coli.
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.
Santos
Sofia Duque
SD
Molecular Neurobiology Unit, Institute for Molecular and Cell Biology, Rua do Campo Alegre 823, Porto, Portugal.
Costa
Rita
R
Teixeira
Pedro Filipe
PF
Gottesman
Max
M
Cardoso
Isabel
I
Saraiva
Maria João
MJ
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
D000682:Amyloid; D029968:Escherichia coli Proteins; D011228:Prealbumin; D013974:Thyroxine