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Related Experiment Videos

High sequence specificity of micrococcal nuclease.

C Dingwall, G P Lomonossoff, R A Laskey

    Nucleic Acids Research
    |June 25, 1981
    PubMed
    Summary

    Micrococcal nuclease preferentially cleaves DNA at A/T-rich sites, not randomly. This enzyme

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    Area of Science:

    • Molecular Biology
    • Enzymology
    • Biochemistry

    Background:

    • Micrococcal nuclease (EC 3.1.4.7.) is widely used as an enzymatic probe in molecular biology.
    • Its "non-specific" nature has been assumed for studying DNA structures like nucleosomes.

    Purpose of the Study:

    • To investigate the substrate specificity of micrococcal nuclease.
    • To determine if micrococcal nuclease is truly a non-specific enzyme for DNA studies.
    • To compare its sequence recognition with other nucleases like DNase I.

    Main Methods:

    • Kinetic analysis of DNA cleavage rates.
    • Digestion of end-labeled linear DNA molecules with known sequences.
    • Analysis of cleavage patterns in supercoiled DNA and nucleosome-assembled DNA.

    Main Results:

    • Micrococcal nuclease exhibits significant sequence specificity, cleaving 30 times more frequently at the 5' side of A or T than G or C.
    • Specific cleavage patterns were observed on end-labeled DNA, influenced by base composition, sequence, and A-T rich regions.
    • Similar sequence preferences were noted in nucleosome-assembled DNA, and micrococcal nuclease mimicked nuclease S1's inverted repeat cleavage.

    Conclusions:

    • Micrococcal nuclease is not a non-specific enzyme and possesses distinct substrate sequence preferences.
    • Its specificity is influenced by nucleotide composition, sequence, and DNA tertiary structure.
    • The use of micrococcal nuclease as a non-specific probe for nucleosome phasing requires re-evaluation due to its inherent sequence bias.

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