Molecular characterization and immunolocalization of Dictyostelium discoideum protein phosphatase 2A.

Protein phosphatase 2A (PP2A) was previously purified from Dictyostelium and biochemically characterized. The purified PP2A holoenzyme was composed of a 37 kDa catalytic 'C-subunit', a 65 kDa 'A-subunit' and a 55 kDa 'B-subunit'. We report here the characterization of the genes encoding the Dictyostelium PP2A subunits as well as the immunolocalization of the PP2A subunits in Dictyostelium. The cDNAs encoding the B- and C-subunits were isolated from a Dictyostelium library and the deduced amino acid sequences reveal strong conservation with the mammalian PP2A homologues. Southern blot analysis suggests that each of the PP2A subunit genes is present in a single copy. The PP2A subunits were localized mainly to the cytosol in Dictyostelium cells. However, immunofluorescence confocal microscopy demonstrates that the B-subunit of PP2A is highly enriched in centrosomes, suggesting a potential role for this PP2A regulatory subunit in the centrosomal function.