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Related Experiment Videos

Splice junctions: association with variation in protein structure.

C S Craik, W J Rutter, R Fletterick

    Science (New York, N.Y.)
    |June 10, 1983
    PubMed
    Summary
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    Intron-exon junctions in eukaryotic genes often align with protein surface loops, potentially explaining functional differences and sequence diversity in enzyme families. This mechanism allows for protein evolution without compromising core stability.

    Area of Science:

    • Genomics
    • Molecular Biology
    • Protein Structure

    Background:

    • Eukaryotic genes contain introns and exons, unlike bacterial genes.
    • Homologous enzymes in bacteria and mammals exhibit sequence and functional variations.
    • Protein structure is crucial for enzyme function.

    Purpose of the Study:

    • To investigate the relationship between intron-exon junctions and protein structure in homologous enzymes.
    • To explore how intron-exon junction positions might explain functional divergence.
    • To identify potential mechanisms for generating protein sequence diversity.

    Main Methods:

    • Comparative analysis of eukaryotic gene sequences and homologous bacterial/mammalian protein sequences.
    • Mapping of intron-exon junctions onto three-dimensional protein structures.

    Related Experiment Videos

  • Analysis of protein surface loops and core stability.

    • Main Results:

    • Intron-exon junctions frequently correspond to variable surface loops in protein structures.
    • Alterations in surface loops due to junction shifts can account for functional differences.
    • Sliding of intron-exon junctions is proposed as a mechanism for generating protein length polymorphisms and sequence divergence.
    • These alterations do not disrupt the stability of the protein core.

    Conclusions:

    • Intron-exon junction positioning is linked to protein surface structure and functional variation.
    • Intron sliding offers a plausible evolutionary mechanism for protein family diversification.
    • This process allows for adaptive changes in protein function without compromising structural integrity.