Three functional luciferase domains in a single polypeptide chain

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...

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Bibliographic Details
Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 94; no. 17; pp. 8954 - 8958
Main Authors:	Li, L.M, Hong, R, Hastings, J.W
Format:	Journal Article
Language:	English
Published:	United States National Academy of Sciences of the United States of America 19-08-1997 National Acad Sciences National Academy of Sciences The National Academy of Sciences of the USA
Subjects:	ADN Amino Acid Sequence AMINO ACID SEQUENCES Amino acids Animals Bacteria Base Sequence Binding Sites - genetics Biochemistry Biological Sciences CHEMICAL COMPOSITION CODE GENETIQUE CODIGO GENETICO CODON USAGE Codons COMPLEMENTARY DNA COMPOSICION QUIMICA COMPOSITION CHIMIQUE Dinoflagellida - enzymology Dinoflagellida - genetics DINOPHYCEAE DINOPHYTA DNA Enzymes Escherichia coli Escherichia coli - genetics Genes GENETIC CODE Genetics GONYAULAX POLYEDRA Light emission Luciferases - chemistry Luciferases - genetics Luciferases - metabolism Marine MOLECULAR SEQUENCE DATA Molecular weight NUCLEOTIDE SEQUENCE Nucleotides OPEN READING FRAMES OXIDOREDUCTASES OXIDORREDUCTASAS OXYDOREDUCTASE PEPTIDE PEPTIDES PEPTIDOS Proteins REPETITIVE DNA Repetitive Sequences, Nucleic Acid SECUENCIA NUCLEOTIDICA Sequence Alignment Sequence Analysis SEQUENCE NUCLEOTIDIQUE
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Summary:	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
Bibliography:	1997061219 F30 M01 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 e-mail: Liming@Hastingslab.Harvard.edu. e-mail: Hastings@Hastingslab.Harvard.edu. Communicated by M. S. Meselson, Harvard University, Cambridge, MA
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.94.17.8954