The structural origin of the color differences in the bioluminescence of firefly luciferase

Six chimeric mutants between Hotaria parvula ( λmax=568 nm) and Pyrocoelia miyako ( λmax=550 nm) luciferases were reconstructed to determine the structural origin of the color differences in firefly luciferase. Based on light-emitting color, five chimeric luciferases could be divided into two groups...

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Veröffentlicht in:	FEBS letters 1996-04, Vol.384 (1), p.83-86
Hauptverfasser:	Ohmiya, Y, Hirano, T, Ohashi, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Active site Amino Acid Sequence Animals Coleoptera Coleoptera - enzymology Color Color difference DNA, Complementary Firefly IPTG, isopropyl β-d-thiogalactopyranoside Lampyridae Light emitting Luciferase Luciferases - biosynthesis Luciferases - chemistry Luciferases - metabolism Luminescence Molecular Sequence Data PCR, polymerase chain reaction Peptide Fragments - chemistry Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Restriction Mapping Sequence Homology, Amino Acid Spectrometry, Fluorescence
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Beschreibung
Zusammenfassung:	Six chimeric mutants between Hotaria parvula ( λmax=568 nm) and Pyrocoelia miyako ( λmax=550 nm) luciferases were reconstructed to determine the structural origin of the color differences in firefly luciferase. Based on light-emitting color, five chimeric luciferases could be divided into two groups: the three green-emitting mutants, classified as P. miyako luciferase, and the two yellow-emitting mutants, classified as H. parvula luciferase. Their common fragments between Val-209 and Ala-318 within each group contain the active site for the color differences.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(96)00288-8