Mutant/mutation
The mutant contains a mutated sams gene where the sams gene has been fused to the destabilizing domain (DD) and a HA tag.

Protein stabilization in vivo was achieved by providing trimethoprim (TMP) in drinking water of mice for 2  days prior to infection (PbSAMS-DD +TMP), while SAMS  conditional knockdown (PbSAMS-DD -TMP) was achieved in non-TMP treated mice, as evidenced by a significant decrease in SAMS-HA-DD protein levels, measured by immunoblotting analysis.

Published in: bioRxiv preprint doi: https://doi.org/10.1101/2022.12.01.518651

Protein (function)
SAMS is the first and rate-limiting enzyme of the methionine cycle. Methionine, among the twenty amino acids, plays an integral role in protein biosynthesis and in regulation of translation and global gene expression - as it is coded by the translation initiation codon. Met is metabolized into S-adenosylmethionine (SAM), the cellular methylation currency, via an ATP-dependent process which is catalyzed by the Plasmodium SAMS enzyme

Phenotype
See below

Additional information
Evidence is presented:
- that fluctuations in AA availability affect parasite growth, by either stalling progression through the intra-erythrocytic asexual cell cycle or by reducing parasite replication rates
- that P. berghei and P. falciparum parasites can actively mount a response to a decrease in two distinct amino acids (AAs) – methionine and isoleucine – by activating in each life cycle stage a different protein kinase, ultimately leading to a reprograming of replication and parasite development. 

Methionine, among the twenty amino acids, plays an integral role in protein biosynthesis and in regulation of translation and global gene expression - as it is coded by the translation initiation codon. Met is metabolized into S-adenosylmethionine (SAM), the cellular methylation currency, via an ATP-dependent process which is catalyzed by the Plasmodium SAMS enzyme.

Other mutants