Properties and developmental regulation of the protein phosphatases in Dictyostelium discoideum.
The properties and developmental regulation of the protein phosphatases of Dictyostelium discoideum were examined. When crude extracts from vegetative cells were separated on a Mono Q column (FPLC) three protein phosphatase peaks, designated P1, P2 and P3 were found. When aggregation and culmination cells were examined only one protein phosphatase peak was observed. This corresponded to phosphatase P1 of vegetative cells. All three of the vegetative cell phosphatase were inhibited by heparin and mammalian phosphatase inhibitor-2, both of which are specific for type-1 protein phosphatases. Trifluoperazine, which inhibits type-2 protein phosphatases, had little effect on any peaks while levamisole, an alkaline phosphatase inhibitor, stimulated P2, slightly inhibited P3 and had no effect on P1. These results demonstrate the existence of two vegetative phase specific protein phosphatases in D. discoideum and one which occurs during all phases of the life cycle. The protein phosphatases isolated from vegetative cells all appear to be type-1 enzymes.
Pamula
F
F
School of Biological Sciences, Flinders University, Bedford Park, Australia.
Wheldrake
J F
JF
D000135:Acid Phosphatase / Q000378:metabolism; D004023:Dictyostelium / Q000201:enzymology* / Q000254:growth & development; D006493:Heparin / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*
D006493:Heparin; D010749:Phosphoprotein Phosphatases; D000135:Acid Phosphatase