Mutant/mutation
The mutant lacks expression of AT1 and expresses GFP under control of a male and RFP under control of a female gametocyte specific promoter.

Protein (function)
Acetyl-CoA participates in post-translational modification of proteins, central carbon and lipid metabolism in several cell compartments. In mammals, the acetyl-CoA transporter 1 (AT1) facilitates the flux of cytosolic acetyl-CoA into the endoplasmic reticulum (ER), enabling the acetylation of proteins of the secretory pathway, in concert with dedicated acetyltransferases including NAT8.
In Plasmodium spp., acetyl-CoA is produced in the mitochondrion atypically through branched-chain α-keto acid dehydrogenase-complex (BCKDH), which uses pyruvate as a substrate. In the apicoplast, a relict plastid organelle derived from secondary endosymbiosis, pyruvate is converted to acetyl-CoA by the pyruvate dehydrogenase complex (PDH), while cytosolic acetyl-CoA is produced through acetyl-CoA synthetase (ACS) from acetate.

Phenotype
Reduced (14x) multiplication/growth of asexual blood stages.
Reduced gametocyte production. In 820cl1PbAT1-KO parasites, an average of 0.6% male gametocytemia compared to 1.32% was observed on day 3 following infection. Nearly no macrogametocytes could be detected in 820cl1PbAT1-KO, with an average of 0.07% compared to 1.71% in wild-type parasites, resulting in an altered sex ratio. The male gametocyte of 820cl1PbAT1-KO also appeared as empty and morphologically different from the wild-type ones through Giemsa staining.
Reduced male gamete formation, defect in axoneme formation, no active exflagellation centers formed. 

Additional information
Proteome-wide analyses revealed widespread N-terminal acetylation marks of secreted proteins in P. berghei. Such acetylation profile of N-terminally processed proteins was never observed so far in any other organisms. In the absence of AT1, the lysine and N-terminal acetylation sites remained globally unaltered, suggesting an uncoupling between the role of AT1 in development and active acetylation occurring along the secretory pathway.
PbAT1 is expressed in both erythrocytic asexual and sexual stages and with a peak of expression at the schizont stage.

Other mutants