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Double-duplication evolution

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In the 1 September Science Lang et al. argue that two single-domain biosynthetic enzymes appear to have evolved from gene duplication, followed by fusion, followed by a second gene duplication (Science 2000, 289:1546-1550). Both of the proteins, HisA and HisF, can be broken down into two half beta/alpha barrels. The four half barrels can be superimposed on each other, revealing 22% identical or similar residues. As both enzymes bind biphosphate substrates, each half barrel has a phosphate-binding motif, and HisF even exhibits limited HisA catalytic activity. Lang et al. propose that an ancestral protein motif was duplicated and fused to produce the HisA isomerase enzyme, before a second duplication and further evolution yielded the more complex HisF synthase activity.

References

  1. 1.

    Science magazine, [http://www.sciencemag.org/]

  2. 2.

    Three-dimensional profiles from residue-pair preferences: identification of sequences with beta/alpha-barrel fold.

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Wells, W. Double-duplication evolution. Genome Biol 1, spotlight-20000906-02 (2000) doi:10.1186/gb-spotlight-20000906-02

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Keywords

  • Catalytic Activity
  • Gene Duplication
  • Protein Motif
  • Biosynthetic Enzyme
  • Ancestral Protein