Mutant/mutation
The mutant lacks expression of RvBL1 (RUVB1)

Protein (function)
In P. yoelii the CCR4-NOT complex is localized in cytoplasmic granules and is involved in translational regulation, playing important roles in development of male and female gametocytes. TRiC and the R2TP (Rvb1–Rvb2–Tah1–Pih1) complex play roles in protein synthesis as chaperones. TRiC is a molecular chaperone that is required for folding of proteins such as actin and tubulin. The R2TP complex is a co-chaperone of HSP90 that assists client proteins to form a large protein complex. Studies have demonstrated that the R2TP complex is essential for the preassembly of dynein arms, an essential step for cilium/flagellum formation.

Phenotype
Two independent parasite clones, in which the RvBL1 gene was disrupted produced mature-appearing females and males. However, both clones lacked exflagellation.

Additional information

From the Abstract:
'Fluorescence microscopy showed that AP2-G expression was first observed in the parasite 12 h after erythrocyte invasion and peaked at 18 h when sexual features were first manifested in  early gametocytes. Expression of  AP2-G decreased with manifestation of  sex-specific features. Chromatin immunoprecipitation followed by sequencing (ChIP-seq) was performed at peak AP2-G expression and identified over 1000 binding sites in the genome. The main binding motif of the TF predicted from the binding sites was GTACNY. Predicted targets contained a number of genes related to protein biogenesis, suggesting that AP2-G plays a role in establishing a cellular basis required for sexual differentiation. AP2-G binding sites also existed upstream of gametocyte-specific TFs, namely AP2-G2, AP2-FG, and AP2-G itself. Furthermore, the target contained two AP2 TF-related genes. Disruption of  these genes resulted in  the arrest of  ookinete development. These results suggest another role of  AP2-G: activating a  transcriptional cascade to  promote conversion into early gametocytes.'

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