Three functional luciferase domains in a single polypeptide chain

Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):8954-8. doi: 10.1073/pnas.94.17.8954.

Abstract

We report a unique case of a gene containing three homologous and contiguous repeat sequences, each of which, after excision, cloning, and expression in Escherichia coli, is shown to code for a peptide catalyzing the same reaction as the native protein, Gonyaulax polyedra luciferase (Mr = 137). This enzyme, which catalyzes the light-emitting oxidation of a linear tetrapyrrole (dinoflagellate luciferin), exhibits no sequence similarities to other luciferases in databases. Sequence analysis also reveals an unusual evolutionary feature of this gene: synonymous substitutions are strongly constrained in the central regions of each of the repeated coding sequences.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites / genetics
  • Dinoflagellida / enzymology
  • Dinoflagellida / genetics*
  • Escherichia coli / genetics
  • Luciferases / chemistry
  • Luciferases / genetics*
  • Luciferases / metabolism
  • Molecular Sequence Data
  • Repetitive Sequences, Nucleic Acid*
  • Sequence Alignment
  • Sequence Analysis

Substances

  • Luciferases

Associated data

  • GENBANK/AF085332