Amyloidogenic properties of transthyretin-like protein (TLP) from Escherichia coli

Santos, Sofia Duque; Costa, Rita; Teixeira, Pedro Filipe; Gottesman, Max; Cardoso, Isabel; Saraiva, Maria João

doi:10.1016/j.febslet.2008.07.025

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Volume 582, Issue 19 , Pages 2893-2898, 20 August 2008

Amyloidogenic properties of transthyretin-like protein (TLP) from Escherichia coli

Edited by Jesus Avila

Sofia Duque Santos
- Molecular Neurobiology Unit, Institute for Molecular and Cell Biology (IBMC),² Rua do Campo Alegre 823, 4150-180 Porto, Portugal
Rita Costa
- Molecular Neurobiology Unit, Institute for Molecular and Cell Biology (IBMC),² Rua do Campo Alegre 823, 4150-180 Porto, Portugal
Pedro Filipe Teixeira
- Molecular Neurobiology Unit, Institute for Molecular and Cell Biology (IBMC),² Rua do Campo Alegre 823, 4150-180 Porto, Portugal
- Present address: Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Max Gottesman
- Institute of Cancer Research, College of Physicians and Surgeons of Columbia University, New York, NY, USA
Isabel Cardoso
- Molecular Neurobiology Unit, Institute for Molecular and Cell Biology (IBMC),² Rua do Campo Alegre 823, 4150-180 Porto, Portugal
Maria João Saraiva
- Molecular Neurobiology Unit, Institute for Molecular and Cell Biology (IBMC),² Rua do Campo Alegre 823, 4150-180 Porto, Portugal
- Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), University of Porto, Portugal
- Corresponding author. Address: Molecular Neurobiology Unit, Institute for Molecular and Cell Biology (IBMC), Rua do Campo Alegre 823, 4150-180 Porto, Portugal. Fax: +351 226099157.

Received 5 June 2008; received in revised form 8 July 2008; accepted 15 July 2008. published online 24 July 2008.

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 8nm width, and annular structures of 8nm diameter which present amyloid-like properties and are toxic to cells.