Mutant/mutation
The mutant lacks expression of glycine cleavage T protein, putative

Protein (function)
The biosynthesis of the active folate factor - N⁵, N¹⁰ - methylenetetrahydrofolate (CH2-THF) that is required for the synthesis of thymidylate and  methionine involves the activities of serine hydroxymethyltransferase (SHMT) and glycine  cleavage system (GCS/GCV; glycine decarboxylase complex).
GCS represents the multi-enzyme complex composed of four proteins namely, P-, H-, T- and L-protein catalyzing the reversible oxidative decarboxylation of glycine to yield carbon dioxide,  ammonia, CH2-THF and reduced nicotinamide adenine dinucleotide.
T-protein, an aminomethyltransferase, represents one of the four components of glycine  cleavage system (GCS) and catalyzes the transfer of methylene group from H-protein intermediate to tetrahydrofolate (THF) forming N⁵, N¹⁰-methylene THF (CH2-THF) with the  release of ammonia. The malaria parasite genome encodes T- (PF3D7_1365500;PBANKA_114130), H- (PF3D7_1132900;PBANKA_091550) and L-proteins (isoform 1: PF3D7_1232200;PBANKA_144690; isoform 2: PF3D7_0815900; PBANKA_071490), but not P-protein which is a glycine decarboxylase generating the aminomethylene group. A putative  GCS has been considered to be functional in the parasite mitochondrion despite the absence of a detectable P-protein homologue.

Phenotype
Phenotype analyses of the knockout mtant indicate that the T-proteins does not play an essential role throughout the life cycle. No phenotypes were detected that were different from wild type parasites.

Additional information
Evidence is presented for a mitochondrial localisation of T-protein in blood stages of both P. falciparum and P. berghei (using antobodies and immunofluorescence analysis).

No detailed information is provided on the generation of the construct. No information is provided for primers (sequence) used to amplify the 3'and 5'UTR target regions.

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