Genetical Research

Research Article

Phosphatase regulation in Aspergillus nidulans: responses to nutritional starvation

Mark X. Caddicka1 p1, Alan G. Brownleea1 p2 and Herbert N. Arst Jra1 p1

a1 Department of Genetics, Ridley Building, The University, Newcastle upon Tyne NE1 7RU, England

SUMMARY

The regulation of the syntheses of a number of phosphatases in the fungus Aspergillus nidulans has been examined. Levels of the intracellular alkaline phosphatase P11 are increased by starvation for carbon, nitrogen, phosphorus or sulphur. There is, however, no evidence that any of the wide domain regulatory genes which mediate sufficiency-triggered repression for each of these elements involved. A possible interpretation is that all four forms of starvation result in accumulation of an inducing metabolite. The palcA gene has been identified as a wide domain, probably positive-acting regulatory gene mediating phosphate repression. The palcA product controls the syntheses of alkaline phosphatase PI, acid phosphatases PIII and PV, a phosphodiesterase lacking phosphomonoesterase activity and probably also a phosphate permease. Mutations resulting in derepression of phosphate-repressible activities at acid but not alkaline growth pH define a gene designated pacJ. pacJ mutations also confer arsenate resistance at low but not high pH. It is likely that phosphate derepression and arsenate resistance result from reduced uptake of H2PO4. Finally, phosphatase regulation might be less complex than previously thought. Mutations designated r and mapping at several loci apparently have no effect on phosphatase. They enhance phosphatase colony staining but this occurs even if the phosphatase substrates are omitted from the staining mixtures. r mutations appear to promote reactions converting the diazonium salts used for phosphatase staining to coloured precipitates.

(Received September 26 1985)

(Revised November 12 1985)

Correspondence:

p1 Present address: Department of Bacteriology, Royal Postgraduate Medical School, Hammersmith Hospital, Ducane Road, London W12 0HS, England.

p2 Present address: CSIRO Division of Animal Production, P.O. Box 239, Blacktown, NSW 2148, Australia.

Footnotes

‡ Address correspondence to this author.

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