Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica

Nur Athirah Yusof, Shazilah Kamaruddin, Farah Diba Abu Bakar, Nor Muhammad Mahadi, Abdul Munir Abd. Murad

Research output: Contribution to journalArticle

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.

Original languageEnglish
JournalCell Stress and Chaperones
DOIs
Publication statusAccepted/In press - 1 Jan 2019

Fingerprint

Chaperonins
Protein Folding
Valine
Alanine
Yeast
Extreme Cold
Substitution reactions
Yeasts
Protein Denaturation
Protein folding
Functional analysis
Denaturation
Isoleucine
Eukaryota
Luciferases
Structural analysis
Hydrogen
Hydrogen bonds
Proteins
Temperature

Keywords

  • CCT
  • Chaperonin
  • Flexibility
  • Molecular chaperone
  • Psychrophiles
  • TCP-1
  • TRiC

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

Cite this

Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica. / Yusof, Nur Athirah; Kamaruddin, Shazilah; Abu Bakar, Farah Diba; Mahadi, Nor Muhammad; Abd. Murad, Abdul Munir.

In: Cell Stress and Chaperones, 01.01.2019.

Research output: Contribution to journalArticle

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