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Functional and morphological stasis during molecular evolution.

R C Williams1

  • 1Department of Anthropology, Arizona State University, Tempe 85287-2402.

American Journal of Physical Anthropology
|January 1, 1990
PubMed
Summary
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Molecular evolution has significantly impacted beta 2-microglobulin, yet murine beta 2-microglobulin still influences human cell antigens. Human and equine alpha-globin show minimal structural divergence.

Area of Science:

  • Molecular Evolution
  • Biochemistry
  • Immunogenetics

Background:

  • Estimating evolutionary distances between proteins is crucial for understanding molecular evolution.
  • Human beta 2-microglobulin and alpha-globin serve as models for studying protein evolution.
  • Kimura's theory of neutral allelic drift provides a framework for interpreting molecular evolution.

Purpose of the Study:

  • To estimate the evolutionary distance between human and murine beta 2-microglobulin.
  • To compare the evolutionary distance between human and equine alpha-globin.
  • To investigate the functional and structural conservation of these proteins despite evolutionary divergence.

Main Methods:

  • Utilized molecular evolutionary techniques from Miyata and Yasunaga (1980) and Kimura (1980).

Related Experiment Videos

  • Compared human beta 2-microglobulin with its murine homolog.
  • Analyzed human and equine alpha-globin sequences.
  • Main Results:

    • Significant molecular evolution observed in beta 2-microglobulin since divergence from a common ancestor.
    • Kimura's evolutionary distance (K) for beta 2-microglobulin: 0.353; Miyata and Yasunaga (KS, KA): 0.708, 0.171.
    • Lower evolutionary distance for human and equine alpha-globin (K: 0.152; KS, KA: 0.293, 0.084).
    • Murine beta 2-microglobulin functionally expressed HLA class I antigens on human-mouse hybrid cells.
    • Human and equine deoxyhemoglobin exhibit nearly identical tertiary structures.

    Conclusions:

    • Despite substantial molecular evolution, beta 2-microglobulin retains functional capacity across species.
    • Conserved tertiary structure in deoxyhemoglobin suggests functional constraints.
    • Findings support Kimura's neutral theory of molecular evolution, indicating a role for neutral drift alongside potential functional selection.