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Amyloidogenic properties of transthyretin‐like protein (TLP) from Escherichia coli
Author(s) -
Santos Sofia Duque,
Costa Rita,
Teixeira Pedro Filipe,
Gottesman Max,
Cardoso Isabel,
Saraiva Maria João
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.07.025
Subject(s) - periplasmic space , transthyretin , escherichia coli , chemistry , monomer , biophysics , peptide , amyloid (mycology) , biochemistry , microbiology and biotechnology , biology , gene , polymer , inorganic chemistry , organic chemistry , endocrinology
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.