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

J Mol Evol. 1990 Feb;30(2):140-5. doi: 10.1007/BF02099940.


A search of sequence databases shows that spherulin 3a, an encystment-specific protein of Physarum polycephalum, is probably structurally related to the beta- and gamma-crystallins, vertebrate ocular lens proteins, and to Protein S, a sporulation-specific protein of Myxococcus xanthus. The beta- and gamma-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 gamma-crystallin domain. The structure of spherulin 3a thus illustrates an earlier stage in the evolution of this protein superfamily. The relationship of beta- and gamma-crystallins to spherulin 3a and Protein S suggests that the lens proteins were derived from an ancestor with a role in stress-response, perhaps a response to osmotic stress.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / genetics*
  • Biological Evolution*
  • Coccidioidin / genetics
  • Crystallins / genetics*
  • Fungal Proteins / genetics
  • Heat-Shock Proteins / genetics
  • Models, Molecular
  • Molecular Sequence Data
  • Myxococcales / genetics
  • Protein Conformation
  • Sequence Homology, Nucleic Acid


  • Bacterial Proteins
  • Crystallins
  • Fungal Proteins
  • Heat-Shock Proteins
  • protein S, Myxococcus xanthus
  • spherulin
  • Coccidioidin