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Related Experiment Videos

Human interstitial retinoid-binding protein. Gene structure and primary structure.

G I Liou1, D P Ma, Y W Yang

  • 1Cullen Eye Institute, Baylor College of Medicine, Houston, Texas 77030.

The Journal of Biological Chemistry
|May 15, 1989
PubMed
Summary
This summary is machine-generated.

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Interstitial retinoid-binding protein (IRBP) gene structure was elucidated, revealing a quadruplicated ancestral gene. This finding provides insights into the evolution of retinoid-binding proteins in photoreceptor cells.

Area of Science:

  • Molecular Biology
  • Genetics
  • Ophthalmology

Background:

  • Interstitial retinoid-binding protein (IRBP) binds retinoids and fatty acids.
  • IRBP is synthesized and secreted by rod photoreceptor cells.

Purpose of the Study:

  • To isolate and characterize the complete human IRBP gene.
  • To investigate the evolutionary origins of the IRBP gene.

Main Methods:

  • Isolation of a 15-kilobase genomic fragment containing the human IRBP gene using cDNA clones.
  • Analysis of gene structure, including introns and coding regions.
  • Deduction of amino acid sequence and analysis of protein homology.

Main Results:

  • The human IRBP gene spans over 11 kilobases with three introns.

Related Experiment Videos

  • The coding region suggests quadruplication of an ancestral gene.
  • The protein sequence shows four homologous segments with up to 60% similarity and conserved glycosylation sites.

    • Conclusions:

    • The human IRBP gene structure provides evidence for gene duplication events in its evolution.
    • Homology to rhodopsin suggests functional relationships in retinal photoreceptor cells.