A cDNA encoding rabbit muscle protein phosphatase 1 alpha complements the Aspergillus cell cycle mutation, bimG11

J. H. Doonan, C. MacKintosh, S. Osmani, P. Cohen, G. Bai, E. Y. Lee, N. R. Morris

    Research output: Contribution to journalArticlepeer-review

    Abstract

    The bimG11 allele causes a conditional growth defect in the fungus Aspergillus nidulans preventing both progression through mitosis and normal polar growth. Previously, we have shown that the bimG11 mutation increases the phosphorylation of nuclear proteins and that the gene encodes a protein similar to mammalian type 1 protein phosphatase. Assay of protein phosphatase activity in protein extracts of Aspergillus demonstrates directly that type 1 phosphatase activity is greatly reduced in the mutant at restrictive temperature. Expression of a muscle type 1 protein phosphatase fully complements all aspects of the bimG11 phenotype, and restores the level of PP1 activity to nearly normal. Expression of the related phosphatase, PP2A, does not complement the bimG11 mutation, showing that complementation can only be achieved by the type 1 gene. This clearly demonstrates that the phenotype of bimG11 is due to reduced PP1 activity and that the PP1 catalytic subunit is functionally conserved over a wide span of evolution.

    Original languageEnglish
    Pages (from-to)18889-18894
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume266
    Issue number28
    Publication statusPublished - 1991

    Cite this