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Related Experiment Videos

Endonucleolytic activity that cleaves immunoglobulin recombination sequences.

T J Hope, R J Aguilera, M E Minie

    Science (New York, N.Y.)
    |March 7, 1986
    PubMed
    Summary

    Researchers found an endonuclease in chick and mouse cells that cuts DNA near immunoglobulin gene recombination sites. This enzyme, which cleaves at TG-AC, is a strong candidate for the enzyme driving V(D)J recombination.

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    Area of Science:

    • Molecular Biology
    • Immunogenetics
    • Cellular Biology

    Background:

    • Immunoglobulin gene rearrangement is crucial for adaptive immunity.
    • V(D)J recombination requires specific DNA cleavage events.
    • The precise endonuclease responsible for initiating V(D)J recombination has remained elusive.

    Purpose of the Study:

    • To identify and characterize an endonuclease activity involved in immunoglobulin gene recombination.
    • To determine the cleavage site specificity of this novel enzyme.
    • To assess its potential role in V(D)J recombination.

    Main Methods:

    • Extraction of nuclear proteins from chick embryo bursa and mouse fetal liver cells.
    • Assay for endonucleolytic activity on DNA substrates mimicking recombination signal sequences.

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  • Characterization of the cleavage site and enzyme properties.

    • Main Results:

    • A novel endonucleolytic activity was detected in nuclear extracts.
    • This activity introduces double-strand breaks near immunoglobulin joining gene segments.
    • Cleavage occurs specifically at the TG-AC dinucleotide sequence.
    • The identified activity is distinct from previously reported endonucleases.

    Conclusions:

    • The characterized endonuclease is a strong candidate for the enzyme initiating V(D)J recombination.
    • Its specific cleavage at TG-AC provides a molecular basis for recombination initiation.
    • This finding advances our understanding of immunoglobulin gene assembly and immune system development.