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Post-translational modification of enzymes: processing genes.

J E Womack

    Isozymes
    |January 1, 1983
    PubMed
    Summary
    This summary is machine-generated.

    Genetic variation in mouse neuraminidase (Neu-1) affects enzyme processing and lysosomal hydrolase activity. This gene

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    Area of Science:

    • Genetics
    • Biochemistry
    • Molecular Biology

    Background:

    • Genomic variation in eukaryotes often arises from genes beyond those encoding primary translation products.
    • Post-translational processing of enzymes is a significant source of allelic variation.
    • Lysosomal hydrolases are enzymes crucial for cellular function, and their processing can be influenced by genetic factors.

    Purpose of the Study:

    • To investigate the role of allelic variation in post-translational enzyme modification.
    • To examine the pleiotropic effects of a specific mouse gene, Neu-1, on lysosomal hydrolases.
    • To map the genetic locus controlling neuraminidase activity and its associated variations.

    Main Methods:

    • Electrophoresis to detect allelic variation in enzyme processing.

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  • Enzyme activity assays to measure neuraminidase levels.
  • Genetic mapping to determine the chromosomal location of the Neu-1 gene.

    • Main Results:

    • Allelic variation in the Neu-1 gene leads to differential sialylation of liver acid phosphatase, alpha-mannosidase, arylsulfatase B, and alpha-glucosidase.
    • Mouse strain SM/J exhibits significantly reduced total neuraminidase activity compared to control strains.
    • The Neu-1 locus is mapped near the H-2 complex on chromosome 17, within the S region.

    Conclusions:

    • Allelic variation in the mouse neuraminidase (Neu-1) gene influences the post-translational modification and activity of multiple lysosomal hydrolases.
    • The Neu-1 gene's location near the H-2 complex suggests potential links to immune function or regulation.
    • Further research is needed to elucidate the precise nature of the mouse Neu-1 mutant and its relevance to human neuraminidase deficiency disorders.