The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin
- PMID: 9346914
- DOI: 10.1074/jbc.272.44.27722
The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin
Abstract
Small heat shock proteins function in a chaperone-like manner to prevent the precipitation of proteins under conditions of stress (e. g. heat). alpha-Crystallin, the major mammalian lens protein, is a small heat shock protein. The mechanism of chaperone action of these proteins is poorly understood. In this paper, the conformational state of a protein when it forms a high molecular weight complex with alpha-crystallin is investigated by examining, using NMR spectroscopy and size exclusion high performance liquid chromatography, the interaction of alpha-crystallin with alpha-lactalbumin and its various intermediately folded (molten globule) states. The complex is formed following reduction of alpha-lactalbumin by dithiothreitol in the presence of alpha-crystallin, and this interaction has been monitored in real time by 1H NMR spectroscopy. It is concluded that alpha-crystallin interacts with a disordered molten globule state of alpha-lactalbumin while it is on an irreversible pathway toward aggregation and precipitation. alpha-Crystallin does not interact, however, with molten globule states of alpha-lactalbumin that are stable in solution, e.g. the reduced and carboxyamidated species. It is proposed that alpha-crystallin distinguishes between the various molten globule states of alpha-lactalbumin on the basis of the lifetimes of these states, i.e. the protein must be in a disordered molten globule state for a significant length of time and on the pathway to aggregation and precipitation for interaction to occur.
Similar articles
-
The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbumin.Biochem Biophys Res Commun. 1998 Aug 28;249(3):917-21. doi: 10.1006/bbrc.1998.9242. Biochem Biophys Res Commun. 1998. PMID: 9731236
-
The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study.J Mol Biol. 2002 May 3;318(3):815-27. doi: 10.1016/S0022-2836(02)00144-4. J Mol Biol. 2002. PMID: 12054825
-
The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin.Biochem J. 2001 Feb 15;354(Pt 1):79-87. doi: 10.1042/0264-6021:3540079. Biochem J. 2001. PMID: 11171082 Free PMC article.
-
The molten globule state of alpha-lactalbumin.FASEB J. 1996 Jan;10(1):102-9. doi: 10.1096/fasebj.10.1.8566530. FASEB J. 1996. PMID: 8566530 Review.
-
Alpha-crystallin as a molecular chaperone.Prog Retin Eye Res. 1999 Jul;18(4):463-509. doi: 10.1016/s1350-9462(98)00030-5. Prog Retin Eye Res. 1999. PMID: 10217480 Review.
Cited by
-
The effects of molecular crowding on the amyloid fibril formation of alpha-lactalbumin and the chaperone action of alpha-casein.Protein J. 2010 May;29(4):257-64. doi: 10.1007/s10930-010-9247-3. Protein J. 2010. PMID: 20496103
-
Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation.Biochem J. 2001 Nov 1;359(Pt 3):547-56. doi: 10.1042/0264-6021:3590547. Biochem J. 2001. PMID: 11672428 Free PMC article.
-
Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins.Protein Sci. 2014 Feb;23(2):229-37. doi: 10.1002/pro.2404. Epub 2013 Dec 16. Protein Sci. 2014. PMID: 24318917 Free PMC article.
-
Human Small Heat Shock Protein B8 Inhibits Protein Aggregation without Affecting the Native Folding Process.J Am Chem Soc. 2023 Jul 19;145(28):15188-15196. doi: 10.1021/jacs.3c02022. Epub 2023 Jul 6. J Am Chem Soc. 2023. PMID: 37411010 Free PMC article.
-
The molecular chaperone β-casein prevents amorphous and fibrillar aggregation of α-lactalbumin by stabilisation of dynamic disorder.Biochem J. 2020 Feb 14;477(3):629-643. doi: 10.1042/BCJ20190638. Biochem J. 2020. PMID: 31939601 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
