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Structural genes for phosphatases in Aspergillus nidulans

Published online by Cambridge University Press:  14 April 2009

Mark X. Caddick  and
Herbert N. Arst Jr
Mark X. Caddick*
Affiliation:
Department of Genetics Ridley Building, The University, Newcastle upon Tyne NE1 7RU, England
Herbert N. Arst Jr*
Affiliation:
Department of Genetics Ridley Building, The University, Newcastle upon Tyne NE1 7RU, England
*
*Address correspondence to this author.
*Address correspondence to this author.
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Although the fungus Aspergillus nidulans has a multiplicity of phosphatases and of genes where mutations affect one or more phosphatases, we have succeeded in identifying structural genes for three phosphatases as well as one other gene which might encode a fourth. Using both conditional and non-conditional mutations, palD has been shown to be the structural gene for a phosphate-repressible alkaline phosphatase, palG to be the structural gene for a non-repressible alkaline phosphatase which apparently exists in two electrophoretically distinct forms (but whose rates of thermal inactivation are apparently very similar) and pacA to be the structural gene for both intracellular and secreted forms of a phosphate-repressible acid phosphatase. Colony staining techniques for the enzymes specified by palD and pacA have been described previously but we have now shown that the enzyme specified by palG can be detected by staining toluene-permeabilized colonies. Mutations in pacG lead to loss of non-repressible acid phosphatase as judged by colony staining and electrophoretic patterns but their effects on assays of activity in cell-free extracts are only marginal. Under phosphate-limited, but not phosphate-starved or phosphate-sufficient, conditions, pacG− mutations also affect the regulation of other, phosphate-repressible phosphatases. None of these phosphatases, alone or in combination, plays an essential role.

Information

Type
Research Article
Information
Genetics Research , Volume 47 , Issue 2 , April 1986 , pp. 83 - 91
Copyright
Copyright © Cambridge University Press 1986

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