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Related Experiment Videos

A myoglobin evolved from indoleamine 2,3-dioxygenase.

T Suzuki1, T Takagi

  • 1Department of Biology, Faculty of Science Kochi University, Japan.

Journal of Molecular Biology
|November 20, 1992
PubMed
Summary
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Abalone myoglobin, a novel protein, challenges the common origin of globins. This unique myoglobin evolved from an indoleamine 2,3-dioxygenase gene, not a globin gene, revealing new evolutionary insights.

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Hemoglobins and myoglobins are well-studied proteins with a presumed common evolutionary origin.
  • These proteins are found across diverse organisms, including animals, plants, and bacteria.
  • Animal globin genes typically exhibit a conserved two-intron, three-exon structure.

Purpose of the Study:

  • To isolate and characterize a novel myoglobin from the abalone Sulculus diversicolor aquatilis.
  • To investigate the evolutionary origin of this unique abalone myoglobin.
  • To understand the functional and evolutionary implications of its sequence homology.

Main Methods:

  • Isolation of myoglobin from abalone red muscle.
  • Determination of the myoglobin's molecular weight and quaternary structure.

Related Experiment Videos

  • cDNA sequencing to derive the amino acid sequence.
  • Bioinformatic analysis to compare homology with known proteins.

    • Main Results:

    • A novel 41 kDa abalone myoglobin was isolated, forming a homodimer.
    • The abalone myoglobin sequence showed no significant homology to other globins.
    • Surprisingly, it exhibited high homology (35% identity) to human indoleamine 2,3-dioxygenase.
    • The abalone myoglobin lacks indoleamine dioxygenase activity but shows accelerated autoxidation in the presence of tryptophan.

    Conclusions:

    • Abalone myoglobin represents a new class of myoglobin, challenging the established globin evolutionary tree.
    • Its evolutionary origin traces back to an indoleamine dioxygenase gene, not a globin gene.
    • The residual tryptophan interaction suggests a molecular relic of its evolutionary past.