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Related Experiment Videos

Evolution of renin.

B J Morris, D F Catanzaro

    Clinical and Experimental Pharmacology & Physiology
    |April 1, 1986
    PubMed
    Summary
    This summary is machine-generated.

    Gene data for aspartyl proteases like human renin and pepsin do not support the gene duplication and fusion hypothesis. Enzyme structure symmetry may stem from amino acid properties at splice junctions.

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Genetics

    Background:

    • Aspartyl proteases, including human renin and pepsin, are crucial enzymes.
    • The gene duplication and fusion hypothesis proposes their evolutionary origin.
    • Understanding their evolution requires detailed gene and sequence analysis.

    Purpose of the Study:

    • To analyze new gene data for human renin, mouse renin, and human pepsin.
    • To investigate the validity of the gene duplication and fusion hypothesis for aspartyl protease evolution.
    • To explore the structural basis for the symmetry observed in aspartyl proteases.

    Main Methods:

    • Sequence alignment of human pepsin hemilobes at amino acid and nucleotide levels.
    • Analysis of splice junctions between putative duplicated exons.

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  • Hybridization studies using labeled human DNA to detect repeated sequences in the human renin gene.

    • Main Results:

    • Weak homology found in amino acid sequences of human pepsin hemilobes; higher nucleotide homology observed.
    • Splice junctions did not align, and repeated sequences in the human renin gene were not consistent with unequal crossing-over.
    • Current data do not support the gene duplication and fusion hypothesis.

    Conclusions:

    • The gene duplication and fusion hypothesis lacks immediate support from the analyzed data.
    • Structural symmetry in aspartyl proteases might be influenced by hydrophilic amino acids at splice junctions.
    • This could lead to the formation of superimposable domains within the enzyme structure.