Abstract and References
Transactions on Science and Technology Vol. 4, No. 3-3, 324 - 329, 2017

Comparative Modeling of TCP1 Ring Complex (TRiC) From a Psychrophilic Yeast, Glaciozyma antarctica

Nur Athirah Yusof, Farah Diba Abu Bakar, Nor Muhammad Mahadi, Abdul Munir Abdul Murad
ABSTRACT
 The TRiC chaperonin belongs to the group II chaperonin that is ubiquitously expressed in the cytosol of archae and eukaryotes. Well known as the complex machinery of protein folding and biogenesis of many cytoskeletal proteins, including tubulin and actin, this chaperonin is indispensable for cell survival as an essential subset of cytosolic proteins requires TRiC for proper folding. Life in extremely cold environment faces energetic challenges to protein folding where psychrophiles have evolved some important cellular adaptations. This indicates that psychrophilic TRiC has undergone positive selection, structural evolution and mechanistic features that distinguish it from other chaperones. The knowledge of this unique complex is in its infancy, therefore we illustrate a systematic tertiary model of the first eukaryotic psychrophilic chaperonin that open the platform to understand the secrets of its folding chamber. The unique ability displayed by the psychrophilic TRiC offers a great opportunity to study the relationship between protein function and structure in terms of stability, flexibility and dynamic conformation.
KEYWORDS: Chaperonin; Glaciozyma antarctica; psychrophile; homology modeling; cylindrical architecture
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