Literature summary for 3.6.4.B10 extracted from

Spillman, N.J.; Beck, J.R.; Ganesan, S.M.; Niles, J.C.; Goldberg, D.E.
The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol (2017), Cell. Microbiol., 19, e12719 .

Search for more literature for 3.6.4.B10

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant ectopic overexpression in in Plasmodium falciparum of each of the N-terminally GFP-tagged PfTRiC subunits, under the expression of the strong, constitutively active HSP86 promoter, the subunits are additionally C-terminally tagged with a ten amino acid flexible linker sequence (PRPGAAHYAA) between the TRiC C-terminus and GFP to avoid disruption of heterohexadecamer formation. All GFP-tagged subunits are successfully overexpressed, except the PfTRiC-zeta subunit, where the GFP signal gets lost	Plasmodium falciparum

Cloned (Comment)

Organism

recombinant ectopic overexpression in in Plasmodium falciparum of each of the N-terminally GFP-tagged PfTRiC subunits, under the expression of the strong, constitutively active HSP86 promoter, the subunits are additionally C-terminally tagged with a ten amino acid flexible linker sequence (PRPGAAHYAA) between the TRiC C-terminus and GFP to avoid disruption of heterohexadecamer formation. All GFP-tagged subunits are successfully overexpressed, except the PfTRiC-zeta subunit, where the GFP signal gets lost

Plasmodium falciparum

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of a regulatable PfTRiC-theta line expressing Myc-tagged subunit theta that forms a large complex in the parasite cytosol, and a theta subunit knockout line. The PfTRiC-theta-MYC clones retain between 4 and 10 aptamer elements. Knockout of PfTRiC-alpha and -zeta subunits using double homologous recombination	Plasmodium falciparum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytoskeleton	upon heat stress, human TRiC-alpha translocates from the cytosolic fraction and associates with the cytoskeleton	Homo sapiens	5856	-
cytosol	chaperonin TRiC forms an heterohexadecameric complex in the malaria parasite cytosol	Plasmodium falciparum	5829	-
cytosol	chaperonin TRiC forms an heterohexadecameric complex in the red blood cell (RBC) cytosol. The stress of parasite infection may lead to translocation of human TRiC subunits from the soluble to insoluble fraction. But the human TRiC-beta and -delta subunits remain in the soluble cytosolic fraction in iRBC. Human TRiC subunits alpha and delta are present in the cytosol of RBC, and this localization is unchanged upon parasite infection	Homo sapiens	5829	-
additional information	the plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction	Plasmodium falciparum	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens
Mg2+	required	Plasmodium falciparum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
550000	-	about, recombinant heterohexadecameric myc-tagged subunit theta complex, native PAGE	Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Homo sapiens	-	ADP + phosphate	-	?
ATP + H2O	Plasmodium falciparum	-	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990	genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta	-
Plasmodium falciparum	Q8II43 AND O97247 AND Q8I5C4 AND C0H5I7 AND O97282 AND C6KST5 AND O77323 AND O96220	genes encoding subunits alpha, beta, gamma, delta, epsilon, zeta, eta, and theta	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
erythrocyte	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Homo sapiens	ADP + phosphate	-	?
ATP + H2O	-	Plasmodium falciparum	ADP + phosphate	-	?

Subunits

Subunits	Comment	Organism
heterohexadecamer	chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol. TRiC is a class II chaperonin, which typically forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings	Homo sapiens
heterohexadecamer	chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol. TRiC is a class II chaperonin, which typically forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings. PfTRiC forms a large complex in the parasite cytosol	Plasmodium falciparum
More	the theta subunit has a molecular weight of 60.9 kDa. The plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction. Loss of one subunit (PfTRiC-theta) in the heterohexadecamer is disrupts formation of the entire complex	Plasmodium falciparum

Synonyms

Synonyms	Comment	Organism
CCT	-	Homo sapiens
CCT	-	Plasmodium falciparum
chaperonin TRiC	-	Homo sapiens
chaperonin TRiC	-	Plasmodium falciparum
HsTRiC	-	Homo sapiens
PfTRiC	-	Plasmodium falciparum
Plasmodium TRiC	-	Plasmodium falciparum
T-complex protein 1	-	Homo sapiens
T-complex protein 1	-	Plasmodium falciparum
T-complex protein 1 ring complex	-	Homo sapiens
T-complex protein 1 ring complex	-	Plasmodium falciparum
TCP-1	-	Homo sapiens
TCP-1	-	Plasmodium falciparum
TriC	-	Homo sapiens
TriC	-	Plasmodium falciparum

General Information

General Information	Comment	Organism
malfunction	knockdown of the PfTRiC-theta subunit is lethal, the lethality is not due to a change in protein export into the host red blood cell (RBC) compartment	Homo sapiens
malfunction	knockdown of the PfTRiC-theta subunit is lethal, the lethality is not due to a change in protein export into the host red blood cell (RBC) compartment. Loss of the PfTRiC complex does not alter export of PfSBP1 or PfREX1. The PfTRiC-theta-MYC clones of teh engineered regulatable line retain between 4 and 10 aptamer elements. The degree of regulation of expression correlates with the number of aptamers in the array, and knockdown reveals that PfTRiC-theta is essential for asexual parasite growth. But loss of one subunit in the heterohexadecamer disrupts formation of the entire complex	Plasmodium falciparum
additional information	human TRiC subunits interact with each other, but do not interact with export related parasite proteins from Plasmodium falciparum in extracts from trophozoite-stage infected red blood cells	Homo sapiens
physiological function	the malaria parasite exports numerous proteins into its host red blood cell (RBC). Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. The parasite TRiC chaperonin complex is exported, and is involved in trafficking of exported effectors. Essential role for PfTRiC within the parasite compartment	Homo sapiens
physiological function	the malaria parasite exports numerous proteins into its host red blood cell (RBC). Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. The parasite TRiC chaperonin complex is exported, and is involved in trafficking of exported effectors. Essential role for PfTRiC within the parasite compartment. Subunit PfTRiC-theta is essential for asexual parasite growth	Plasmodium falciparum