Journal of Molecular Evolution

, Volume 30, Issue 2, pp 140–145

Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins

  • Graeme Wistow
Article

DOI: 10.1007/BF02099940

Cite this article as:
Wistow, G. J Mol Evol (1990) 30: 140. doi:10.1007/BF02099940

Summary

A search of sequence databases shows that spherulin 3a, an encystment-specific protein ofPhysarum polycephalum, is probably structurally related to the β- and γ-crystallins, vertebrate ocular lens proteins, and to Protein S, a sporulation-specific protein ofMyxococcus xanthus. The β- and γ-crystallins have two similar domains thought to have arisen by two successive gene duplication and fusion events. Molecular modeling confirms that spherulin 3a has all the characteristics required to adopt the tertiary structure of a single γ-crystallin domain. The structure of spherulin 3a thus illustrates an earlier stage in the evolution of this protein superfamily. The relationship of β- and γ-crystallins to spherulin 3a and Protein S suggests that the lens proteins were derived from an ancestor with a role in stressresponse, perhaps a response to osmotic stress.

Key words

Lens crystallinsPhysarum polycephalumSpherulinsProtein evolutionStress

Copyright information

© Springer-Verlag New York Inc. 1990

Authors and Affiliations

  • Graeme Wistow
    • 1
  1. 1.LMDB, National Eye InstituteNational Institutes of HealthBethesdaUSA