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A sequence specific endonuclease from Micrococcus radiodurans.

A A Wani, R E Stephens, S M D'Ambrosio

    Biochimica Et Biophysica Acta
    |May 31, 1982
    PubMed
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    Researchers purified a new restriction enzyme, Mra I, from Micrococcus radiodurans. This enzyme, an isoschizomer of Sac II and Sst II, recognizes a specific DNA sequence and has unique cleavage sites on bacteriophage lambda DNA.

    Area of Science:

    • Molecular Biology
    • Enzymology
    • Microbiology

    Background:

    • Restriction enzymes are crucial tools in molecular biology for DNA manipulation.
    • Identifying novel restriction enzymes expands the toolkit for genetic engineering and research.
    • Micrococcus radiodurans is a bacterium known for its radiation resistance, suggesting unique enzymatic properties.

    Purpose of the Study:

    • To purify and characterize a novel sequence-specific endonuclease from Micrococcus radiodurans.
    • To determine the cleavage specificity and properties of the new enzyme, Mra I.
    • To investigate the potential of Mra I as a unique tool in molecular biology.

    Main Methods:

    • Purification of Mra I from Micrococcus radiodurans.
    • DNA cleavage assays using various viral and plasmid DNA substrates (bacteriophage lambda, adenovirus type 2, phi X174, SV40, PM2, pBR322).

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  • Determination of cleavage site locations on lambda DNA.
  • Enzyme activity analysis under different conditions (pH, temperature, cofactors).
  • Comparison with known restriction enzymes (isoschizomer identification).

    • Main Results:

    • Mra I was purified and characterized as a sequence-specific endonuclease.
    • The enzyme exhibits unique cleavage patterns on different DNA molecules.
    • Cleavage sites on lambda DNA were mapped to specific fractional lengths.
    • Mra I was identified as an isoschizomer of Sac II and Sst II, recognizing the sequence 5'-CCGC/GG-3'.
    • Optimal activity was observed at 45°C and pH 7.0, with an absolute requirement for Mg2+.
    • The enzyme functions without added 2-mercaptoethanol.

    Conclusions:

    • Mra I is a novel restriction enzyme with specific DNA cleavage properties.
    • Its unique recognition sequence and cleavage sites offer new possibilities for DNA analysis.
    • Mra I is the first reported restriction enzyme from a bacterium lacking modified methylated bases.
    • This discovery contributes to the understanding of restriction-modification systems and provides a valuable new enzyme for molecular biology applications.