Mutant/mutation
The mutant  expresses a mutated form of of the RNA binding protein Puf2.
The predominant feature of Puf2 is its RNA binding domain (RBD), which is comprised of eight canonical RNA recognition helices. The mutated Puf2 lacks the N-terminal domain by fusing the Puf2 5′ UTR (including its start codon) to the predicted RBD and spans all four exons (AA132-478). The N-terminal portion of Puf2 (AA1-131) has no predicted PFAM domains, nor any significant similarity/identity to non-orthologous proteins. The mutated Puf2 also contains a C-terminal 4x Myc tag to the RBD.

Protein (function)
The roles of Puf (Pumilio and fem-3 mRNA binding factor) proteins are diverse yet intimately involved in the translational regulation of developmental and differentiation factors in organisms as diverse as yeast, C. elegans, Drosophila and humans. Two such proteins, Puf1 (PFE0935c) and Puf2 (PFD0825c), are known in the human malaria parasite, P. falciparum, with orthologs in all Plasmodium spp. characterized. The Plasmodium Puf proteins have the typical highly conserved organization that includes the eight tandem copies of the PUM RNA binding domain (or Pumilio Homology Domain, PHD) at the carboxyterminus of the protein and expectedly PfPuf2 was shown to bind RNA in vitro. In P. falciparum evidence has been reported for a role for Puf2 in gametocyte development although Pfpuf2 is most highly transcribed in sporozoites.
Analysis of P. berghei RMgm-515, RMgm-516, RMgm-617) and P. yoelii (RMgm-842) mutants lacking expression of Puf2 indicate that  Puf2 regulates the transition of sporozoites into liver stage forms.

Phenotype
Analysis of P. berghei RMgm-515, RMgm-516, RMgm-617) and P. yoelii (RMgm-842) mutants lacking expression of Puf2 indicate that  Puf2 regulates the transition of sporozoites into liver stage forms. Sporozoites lacking expression of Puf2 show reduced infectivity.

Analysis of the mutant expressing the mutated form of Puf2 indicates that  the RNA binding domain (RBD) is necessary and sufficient for all essential Puf2 functions, and parasites that express only the RBD retain normal infectivity and exhibit no phenotypic defects.

Additional information
By analysis of  Puf2 localisation in sporozoites evidence is presented that Puf2 traffics to sporozoite cytosolic granules, which are negative for several markers of stress granules and P-bodies, and disappear rapidly after infection of hepatocytes.
RNAseq analyses provided evidence for a role of Puf2 in directly or indirectly maintaining the homeostasis of specific transcripts in sporozoites.

Other mutants
P. berghei mutants that lack expression of Puf2: RMgm-515, RMgm-516, RMgm-617)
RMgm-842: a P. yoelii mutant lacking expression of Puf2