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Related Experiment Videos

Restriction endonuclease EcaI from Enterobacter cloacae.

G Hobom, E Schwarz, M Melzer

    Nucleic Acids Research
    |October 10, 1981
    PubMed
    Summary

    Restriction endonuclease EcaI from Enterobacter cloacae recognizes specific DNA sequences and creates fragments with extensions. This enzyme shows identical specificity to BstEII, aiding in molecular biology applications.

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    Clinical biomechanics (Bristol, Avon)·2018

    Area of Science:

    • Molecular Biology
    • Enzymology
    • Genetics

    Background:

    • Restriction endonucleases are crucial tools in molecular biology for DNA manipulation.
    • Understanding enzyme specificity is key for precise genetic engineering and analysis.
    • Enterobacter cloacae DSM30056 produces the restriction enzyme EcaI.

    Purpose of the Study:

    • To characterize the DNA recognition sequence and cleavage pattern of restriction endonuclease EcaI.
    • To compare the specificity of EcaI with other known restriction enzymes.

    Main Methods:

    • DNA sequencing and analysis to determine the recognition site.
    • Enzymatic digestion assays to observe cleavage products.
    • Comparison of EcaI activity with restriction endonuclease BstEII.

    Main Results:

    • Restriction endonuclease EcaI recognizes the heptanucleotide palindrome 5'-G[unk]G-T-N-A-C-C-3'.
    • EcaI cleavage results in fragments with 5'-terminal pentanucleotide extensions.
    • EcaI exhibits identical specificity to restriction endonuclease BstEII.

    Conclusions:

    • EcaI is a valuable restriction enzyme with a defined specificity profile.
    • The identical specificity of EcaI and BstEII offers flexibility in molecular cloning strategies.
    • This characterization expands the toolkit for DNA manipulation in biotechnology.

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