Amyloid fibril formation by a helical cytochrome

FEBS Letters

Dobson, Christopher M.¹  Wain, Rachel¹  Tomlinson, Esther J.²  Ferguson, Stuart J.²  Pertinhez, Thelma A.¹  Smith, Lorna J.¹  Bouchard, Mario¹ 

[1] New Chemistry Laboratory, Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford OX1 3QT, UK;Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK

关键词: Cytochrome c 552;    Amyloid fibril;    Circular dichroism;    Electron microscopy;    CD;    circular dichroism;   

DOI  :  10.1016/S0014-5793(01)02384-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The substitution of alanines for the two cysteines which form thioether linkages to the haem group in cytochrome c ₅₅₂ from Hydogenobacter thermophilus destabilises the native protein fold. The holo form of this variant slowly converts into a partially folded apo state that over prolonged periods of time aggregates into fibrillar structures. Characterisation of these structures by electron microscopy and thioflavin-T binding assays shows that they are amyloid fibrils. The data demonstrate that when the native state of this cytochrome is destabilised by loss of haem, even this highly α-helical protein can form β-sheet structures of the type most commonly associated with protein deposition diseases.

【 授权许可】

Unknown