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[Intercellular serine proteinases from spore-forming bacilli]

A Ia Strongin, V M Stepanov

    Biokhimiia (Moscow, Russia)
    |August 1, 1981
    PubMed
    Summary

    Intracellular serine proteinases in spore-forming bacilli share evolutionary links with secretory subtilisins. Their unique dimeric structure and rapid evolution suggest distinct functional roles in microorganisms like Escherichia coli.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Evolutionary Biology

    Background:

    • Intracellular serine proteinases are crucial enzymes found across diverse microorganisms.
    • These enzymes are structurally and evolutionarily related to secretory subtilisins.
    • Understanding their unique properties is key to comprehending microbial enzymatic functions.

    Purpose of the Study:

    • To investigate the physico-chemical, immunological, structural, functional, and evolutionary characteristics of intracellular serine proteinases from spore-forming bacilli.
    • To compare these intracellular enzymes with secretory subtilisins.
    • To elucidate the evolutionary pathways and genetic basis of these proteinases.

    Main Methods:

    • Comparative analysis of physico-chemical properties.
    • Immunological reaction studies.
    • Structural and functional characterization.
    • Evolutionary feature assessment.

    Main Results:

    • Intracellular serine proteinases form a distinct subfamily, closely related to secretory subtilisins in structure and evolution.
    • These enzymes exhibit a faster evolutionary rate than secretory subtilisins due to stringent selective control.
    • Active intracellular proteinases possess a unique dimeric structure preventing random proteolysis.
    • Separate, related genes code for intracellular bacillary serine proteinases and secretory subtilisins, likely arising from gene duplication.

    Conclusions:

    • Intracellular serine proteinases and secretory subtilisins originate from a common precursor gene, evidenced by gene duplication.
    • The dimeric structure of intracellular proteinases is vital for maintaining cellular proteostasis.
    • The accelerated evolution of these enzymes reflects adaptation to specific intracellular environments and functions.

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