Temperature‐induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α‐crystallin
- 7 August 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 369 (2-3) , 321-325
- https://doi.org/10.1016/0014-5793(95)00775-5
Abstract
Alpha-Crystallin, the major protein of the ocular lens, is known to have extensive similarities to small heat shock proteins and to act as a molecular chaperone. The exposure of hydrophobic surfaces on alpha-crystallin was studied by fluorescence spectroscopy using the hydrophobic probe bis-ANS. Upon heating the protein undergoes a conformational transition which is associated with a marked increase in surface hydrophobicity. This transition, which occurs between approximately 38 and 50 degrees C, lacks reversibility. The increase in surface hydrophobicity correlates with the increased chaperone activity of the protein. These results indicate that hydrophobic interactions play a major role in the chaperone action of alpha-crystallin.Keywords
This publication has 29 references indexed in Scilit:
- Thermodynamic Partitioning Model for Hydrophobic Binding of Polypeptides by GroEL: I. GroEL Recognizes the Signal Sequences of β-lactamase PrecursorJournal of Molecular Biology, 1994
- The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin‐assisted foldingFEBS Letters, 1994
- Membrane interactions and surface hydrophobicity of Bacillus thuringiensis δ‐endotoxin CryICFEBS Letters, 1994
- Expression of the α‐Crystallin/Small Heat‐Shock Protein/Molecular Chaperone Genes in the Lens and other TissuesPublished by Wiley ,1994
- Hsp85 conformational change within the heat shock temperature rangeBiochemical and Biophysical Research Communications, 1992
- Heat‐induced changes in the conformation of α‐ and β‐crystalline: Unique thermal stability of α‐crystallinFEBS Letters, 1988
- A possible structure for α‐crystallinFEBS Letters, 1987
- Calf lens α-crystallin quaternary structureJournal of Molecular Biology, 1986
- Domain structure and evolution in α‐crystallins and small heat‐shock proteinsFEBS Letters, 1985
- Preparation, crystalline structure, and spectral properties of the fluorescent probe 4,4'-bis-1-phenylamino-8-naphthalenesulfonateJournal of the American Chemical Society, 1978