Mutant/mutation
The mutant expresses a C-terminal GFPmut2-tagged version of ALBA4.

Protein (function)
ALBA proteins are evolutionarily conserved from Archaea and consistently have been found to bind to nucleic acids. Structurally, the ALBA domain resembles the IF3 C-terminal domain, which binds to the small subunit of the prokaryotic ribosome. Together, this strategy provides a straightforward mechanism for ALBA proteins to tether nucleic acids to the ribosome. Plasmodium spp. contain at least four ALBA-domain containing proteins, and have been shown to bind both DNA and RNA. Of these ALBA proteins, ALBA4 is specific to the Apicomplexan lineage and its Chromerid ancestor (40-50%; identity / 60-65% similarity).

Phenotype
See mutant RMgm-4313 for a mutant lacking expression of ALBA4.
Fusion of GFPmut2 to PyALBA4 did not result in any detectable morphological or phenotypical effects compared to the WT-GFP parasite line at any point of the life cycle.
PyALBA4 is expressed throughout asexual blood stage development. PyALBA4 traffics to cytosolic puncta in ring, trophozoite, and schizont stages, and can be found as nuclear adjacent foci, near the cell periphery, and at all points between.
In gametocytes PyALBA4 is abundantly expressed, and can be found both diffusely and in puncta in the cytoplasm in both male and female gametocytes.
PyALBA4 is expressed diffusely throughout early oocysts (Day 3) but then much of it is directed to puncta within developing sporozoites, with the remainder persisting within sporoblasts/cytoplasmic islands.
Sporozoites liberated from the oocyst (Day 10) retain only a few puncta of PyALBA4, which are largely nuclear adjacent. Salivary gland sporozoites (Day 14) contain far more PyALBA4 granules, which extend from near the nucleus out to both ends of the parasite.
PyALBA4 expression/localisation shifts from a largely diffuse expression pattern in mid-liver stage (24 hours) to increasingly smaller puncta during late (48 hours) and very late (52 hours) liver stage.

Additional information
Immunoprecipitation studies were performed using GFP-tagged ALBA4 identifying a number of proteins as putative interacting partners of ALBA4, for example Musashi, Bruno, GBP2, SR1, GAPDH, Aldolase, PABP, a thioredoxin peroxidase, EF1alpha, ribosomal proteins and ALBA1, 2, 3, and 4. The authors conclude: 'the interactions with  ribosome-associated factors are in agreement with previous work that showed that the ALBA domain resembles the IF3-C domain that interacts with the small subunit of the ribosome, and other work that showed that a a member of this complex in yeast (ScDHH1) associates directly with the ribosome.

Other mutants
Mutant RMgm-4313: a mutant lacking expression of ALBA4