Three functional luciferase domains in a single polypeptide chain

Liming Li*, Robert Hong, J. Woodland Hastings

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

57 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)8954-8958
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number17
StatePublished - Aug 19 1997

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Three functional luciferase domains in a single polypeptide chain'. Together they form a unique fingerprint.

Cite this