Inclusion body formation by interleukin‐1β depends on the thermal sensitivity of a folding intermediate

FEBS Letters

Wetzel, Ronald¹  Chrunyk, Boris A¹ 

[1] Macromolecular Sciences Department, UE0447D, SmithKline Beecham Pharmaceuticals, 709 Swedeland Road, King of Prussia, PA 19406, USA

关键词: Inclusion body;    Mutation;    Interleukin-1β;    Folding intermediate;    Temperature-sensitive folding;    Folding kinetics;    Hydrophobicity;   

DOI  :  10.1016/0014-5793(94)00775-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We show that sequence and growth temperature effects on IB formation in the small, monomeric β-barrel protein interleukin-1β (IL-1β) can be quantitatively reproduced in an in vitro system in which IL-1β is refolded from denaturant at different temperatures. The results suggest that temperature and mutational effects on IB formation may be based on intrinsic properties of the protein sequence rather than interactions with chaperones or other cellular factors. We also report striking correlations of IB formation with mutation-dependent changes in residue hydrophobicity. The nature of these trends differs considerably with residue position, however, suggesting that they are mediated by particular local environments created by an ordered structure.

【 授权许可】

Unknown