Abstract
Studies on TCP1-1 ring complex (TRiC) chaperonin have shown its indispensable role in folding cytosolic proteins in eukaryotes. In a psychrophilic organism, extreme cold temperature creates a low-energy environment that potentially causes protein denaturation with loss of activity. We hypothesized that TRiC may undergo evolution in terms of its structural molecular adaptation in order to facilitate protein folding in low-energy environment. To test this hypothesis, we isolated G. antarctica TRiC (GaTRiC) and found that the expression of GaTRiC mRNA in G. antarctica was consistently expressed at all temperatures indicating their importance in cell regulation. Moreover, we showed GaTRiC has the ability of a chaperonin whereby denatured luciferase can be folded to the functional stage in its presence. Structurally, three categories of residue substitutions were found in α, β, and δ subunits: (i) bulky/polar side chains to alanine or valine, (ii) charged residues to alanine, and (iii) isoleucine to valine that would be expected to increase intramolecular flexibility within the GaTRiC. The residue substitutions observed in the built structures possibly affect the hydrophobic, hydrogen bonds, and ionic and aromatic interactions which lead to an increase in structural flexibility. Our structural and functional analysis explains some possible structural features which may contribute to cold adaptation of the psychrophilic TRiC folding chamber.
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Acknowledgments
We are grateful to the Ministry of Science, Technology and Innovation, Malaysia, (MOSTI) for funding our project under grant number 02-05-20-SF0007. We thank Prof Jamie Rossjohn for the opportunity to use his lab at Monash University and synchrotron facilities in Australia. Special thanks to Dr. Travis Beddoe from La Trobe University who assisted us with his advice and technical guidance. We are thankful to the Ministry of Higher Education Malaysia for the FRG0463-2017 grant for funding the continuous culturing of Glaciozyma antarctica in Biotechnology Research Institute, Universiti Malaysia Sabah. We also thank those who were involved in the structural project of Glaciozyma antarctica in Malaysia Genome Institute and others who assisted with technical assistance and helpful discussions.
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Yusof, N.A., Kamaruddin, S., Abu Bakar, F.D. et al. Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica. Cell Stress and Chaperones 24, 351–368 (2019). https://doi.org/10.1007/s12192-019-00969-1
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DOI: https://doi.org/10.1007/s12192-019-00969-1