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Molecular chaperones are generally proteins, which assist other unrelated proteins to achieve their correct fate in vivo, be that proper folding, oligomeric assembly, subcellular localization, etc. It is not yet known what features of a protein make it a chaperone. Since both protein and non-protein molecules are now known to function as chaperones, we have compared the structural features of many known chaperones to identify common distinctive feature. Our study reveals that many known chaperones have a micelle type organization as a common feature. Even non-protein chaperones have similar structural features. Other factors such as possession of hydrophobic and hydrophilic domains, flexibility of the structure and solubilising capacity of the protein are also important. Based on these features we predicted that tubulin and a random coil protein, α_s-casein may possess chaperone-like activity. These predictions have been verified by experiments in our laboratory and our results clearly show that both tubulin and casein acts as effective molecular chaperones.

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Structural Stabilization and Functional Enhancement of Miceller Protein α-Crystallin by ATP and Zn2+

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Authors

Srabani Karmakar ¹, Ashis Biswas ¹, K. P. Das ¹

Affiliations
1 Protein Chemistry Laboratory, Department of Chemistry, Bose Institute, 93/1 A.P.C. Road, Kolkata - 700 009, West Bengal, IN

Source

Journal of Surface Science and Technology, Vol 31, No 1-2 (2015), Pagination: 13-20

Abstract

α-Crystallin is the most abundant protein of the eye lens. It has a micelle like associated structure and has a special chaperone- like property to prevent aggregation of other proteins. This function of α-crystallin plays a crucial role in maintaining the transparency of eye lens. Because of the absence of protein turn over in the lens, the proteins in the lens must survive the entire lifetime of the living species. This requires high structural stability of α-crystallin. In this article we present a brief review of our work on the mechanism of stabilization of α-crystallin by Zn. We have shown that some metal ions, Zn in particular play a very important role in enhancing the function of α-crystallin by enhancing its exposed hydrophobic surface. We have also characterized the Zn binding to α-crystallin by MALDI mass spectrometry and have shown that the structural stabilization occurs through intersubunit bridging by Zn. The binding region in the α-crystallin sequence has also been identified. The physiological relevance of enhanced chaperone function and structural stability is discussed.

Keywords

Alpha Crystallin, Chaperone Function, Eye Lens Protein, Metal Binding, Miceller Protein, Protein Aggregation

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