title: Three functional luciferase domains in a single polypeptide chain.
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.
authors.affiliation: Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138-2020, USA. Liming@Hastingslab.Harvard.edu
authors.forename: L
authors.initials: L
authors.lastname: Li
authors.forename: R
authors.initials: R
authors.lastname: Hong
authors.forename: J W
authors.initials: JW
authors.lastname: Hastings
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D004141:Dinoflagellida / Q000201:enzymology / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics; D008156:Luciferases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D012091:Repetitive Sequences, Nucleic Acid; D016415:Sequence Alignment; D017421:Sequence Analysis
chemical_list: D008156:Luciferases