Abstract
Tubulin polymerization promoting proteins (TPPPs) belong to a family of neomorphic moon lighting proteins, involved in various physiological and pathological conditions. In physiological conditions, TPPPs play an important role in microtubule dynamics regulating mitotic spindle assembly and in turn cell proliferation. In pathological situations, TPPPs interact with α-synuclein and β-amyloid and promote their aggregation leading to Parkinson's disease and multiple system atrophy. Orthologs of TPPP family proteins were identified in ciliary proteomes from various organisms including Chlamydomonas but their role in ciliogenesis was not known. Here we showed that Flagellar Associated Protein, FAP265, a Chlamydomonas homologue of TPPP family proteins, localizes in the cytosol, at the basal bodies and in the flagella of vegetative Chlamydomonas cells. During cell division, the protein was found as a distinct spot in the nucleus and at the cleavage furrow which forms between the daughter cells. Further null mutants of Chlamydomonas FAP265 protein, fap265, showed severe defects in hatching from the mother sporangium. Daughter cells of fap265 were significantly larger in size compared with wild type cells. Moreover, the daughter cells present within the mother sporangium failed to form flagella before hatching. They reassembled their flagella only after hatching from the sporangium suggesting that FAP265 plays an important role in flagellar reassembly after cell division.