Literature summary for 3.6.4.B10 extracted from

Yusof, N.A.; Kamaruddin, S.; Abu Bakar, F.D.; Mahadi, N.M.; Abdul Murad, A.M.
Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica (2019), Cell Stress Chaperones, 24, 351-368 .

Search for more literature for 3.6.4.B10

Cloned(Commentary)

Cloned (Comment)	Organism
genes encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta, DNA and amino acid sequence determination, sequences comparisons, quantitative real-time PCR expression analysis at different temperatures, overview. GaTRiC subunits are constitutively expressed at all temperatures with the exception of GaTRiCbeta subunit at 20°C reaching 4.5fold expression compared to optimal growth at 12°C	Glaciozyma antarctica

Cloned (Comment)

Organism

genes encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta, DNA and amino acid sequence determination, sequences comparisons, quantitative real-time PCR expression analysis at different temperatures, overview. GaTRiC subunits are constitutively expressed at all temperatures with the exception of GaTRiCbeta subunit at 20°C reaching 4.5fold expression compared to optimal growth at 12°C

Glaciozyma antarctica

Protein Variants

Protein Variants	Comment	Organism
additional information	three categories of residue substitutions are found in alpha, beta, and gamma subunits: (i) bulky/polar side chains to alanine or valine, (ii) charged residues to alanine, and (iii) isoleucine to valine that is expected to increase intramolecular flexibility within the GaTRiC	Glaciozyma antarctica

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Glaciozyma antarctica

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Glaciozyma antarctica	-	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Glaciozyma antarctica	A0A1S6LQX4 AND A0A1S6LQU3 AND A0A1S6LQU0 AND A0A1S6LQU6 AND A0A1S6LQU1 AND A0A1S6LQU9 AND A0A1S6LQW6 AND A0A1S6LQW7	genes encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta	-

Purification (Commentary)

Purification (Comment)	Organism
native enzyme by anion exchange chromatography and gel filtration	Glaciozyma antarctica

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	GaTRiC is consistently expressed at all temperatures	Glaciozyma antarctica	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Glaciozyma antarctica	ADP + phosphate	-	?
additional information	GaTRiC acts a chaperonin mediating folding of denatured luciferase to the functional stage	Glaciozyma antarctica	?	-	-

Subunits

Subunits	Comment	Organism
heterohexadecamer	TRiC forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings	Glaciozyma antarctica

Synonyms

Synonyms	Comment	Organism
CCT	-	Glaciozyma antarctica
chaperonin containing t-complex polypeptide-1	-	Glaciozyma antarctica
GaTRiC	-	Glaciozyma antarctica
T-complex protein 1	-	Glaciozyma antarctica
TriC	-	Glaciozyma antarctica

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
4	-	refolding/ATPase	Glaciozyma antarctica

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
-	30	activity range, profile overview	Glaciozyma antarctica

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	refolding/ATPase assay at	Glaciozyma antarctica

General Information

General Information	Comment	Organism
malfunction	three categories of residue substitutions are found in alpha, beta, and gamma subunits: (i) bulky/polar side chains to alanine or valine, (ii) charged residues to alanine, and (iii) isoleucine to valine that is 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	Glaciozyma antarctica
additional information	structure-functional analysis, the three-dimensional structure of GaTRiC is modeled using the Saccharomyces cerevisiae TRiC structure (PDB ID 4V81) as template. Determination of ionic interactions of GaTRiC residues	Glaciozyma antarctica
physiological function	the chaperonin containing t-complex polypeptide-1 which is also known as TRiC plays a central role in cellular homeostasis by facilitating the folding of approximately 10% or more of newly synthesized proteins which include tubulins, actins, luciferin, Von Hippel-Lindau disease tumor suppressor (VHL), histone deacetylase 3, and other client proteins. Enzyme GaTRiC is important in cell regulation	Glaciozyma antarctica