Cloning, sequence analysis, and expression of active Phrixothrix railroad-worms luciferases: relationship between bioluminescence spectra and primary structures.

@article{Viviani1999CloningSA,
  title={Cloning, sequence analysis, and expression of active Phrixothrix railroad-worms luciferases: relationship between bioluminescence spectra and primary structures.},
  author={Vadim Ravara Viviani and Eteivino J. H. Bechara and Yoshihiro Ohmiya},
  journal={Biochemistry},
  year={1999},
  volume={38 26},
  pages={
          8271-9
        }
}
Phrixothrix railroad-worms emit yellow-green light through 11 pairs of lateral lanterns along the body and red light through two cephalic lanterns. The cDNAs for the lateral lanterns luciferase of Phrixothrix vivianii, which emit green light (lambda max= 542 nm), and for the head lanterns of P. hirtus, which emit the most red-shifted bioluminescence (lambda max= 628 nm) among luminescent beetles, were cloned. Positive clones which emitted green (PvGR: lambda max= 549 nm) and red (PhRE: lambda… 
Bioluminescence Color Determinants of Phrixothrix Railroad-worm Luciferases: Chimeric Luciferases, Site-directed Mutagenesis of Arg 215 and Guanidine effect¶
TLDR
Guanidine was shown to cause blueshifts in the BL spectra and stimulate the activity of the red-emitting luciferases and in PxGr R215S mutant luciferase, but not in the green-emmittingLuciferases, suggesting that guanidine can simulate positively charged residues involved in BL color determination.
Bioluminescence Color Determinants of Phrixothrix Railroad‐worm Luciferases: Chimeric Luciferases, Site‐directed Mutagenesis of Arg 215 and Guanidine effect ¶
TLDR
Guanidine was shown to cause blueshifts in the BL spectra and stimulate the activity of the red‐emitting luciferases and in PxGr R215S mutant luciferase, but not in the green-emittingLuciferases, suggesting that guanidine can simulate positively charged residues involved in BL color determination.
Active-site properties of Phrixotrix railroad worm green and red bioluminescence-eliciting luciferases.
TLDR
Cloned luciferases of the railroad worm Phrixotrix are cloned and several invariant residues in the putative luciferin-binding site of the red-emitting PxRE luciferase cannot interact with excited oxyluciferin.
Molecular insights on the evolution of the lateral and head lantern luciferases and bioluminescence colors in Mastinocerini railroad-worms (Coleoptera: Phengodidae).
TLDR
The results suggest that the head and lateral lanterns luciferases in Mastinocerini are coded by paralogous genes, and that the ancestral luciferase in the Phengodinae subfamily produced green bioluminescence.
Thr226 is a key residue for bioluminescence spectra determination in beetle luciferases.
TLDR
Data suggest that Thr226 is an important residue for keeping active-site core in both groups of beetle luciferases and the mechanism for bioluminescence color determination between pH-sensitive and pH-insensitiveLuciferases could be different.
Cloning,Expression and Sequence Analysis of A Luciferase Gene from the Chinese Firefly Pyrocoelia pygidialis
TLDR
Five loops in the P.pygidialis luciferase, L1(N198-G208), L2(T240-G247), L3(G317-K322), L4(L343-I350) and L5(G522-D532), were found from the structure modeling analysis in the cleft, where it was considered the active site for the substrate compound entering and binding.
Second Rhagophthalmid Luciferase Cloned from Chinese Glow‐worm Menghuoius giganteus (Rhagophthalmidae: Elateroidea)
TLDR
The second rhagophthalmid luciferase from the Chinese glow‐worm Menghuoius giganteus is cloned by combining reverse transcription polymerase chain reaction (RT‐PCR) with rapid amplification of complementary DNA ends (RACE) andylogenetic analyses indicated a close relationship with that of R. ohbai.
The Influence of the Loop between Residues 223‐235 in Beetle Luciferase Bioluminescence Spectra: A Solvent Gate for the Active Site of pH‐Sensitive Luciferases
TLDR
It is shown that substitutions dramatically affecting bioluminescence colors in both groups of luciferases are clustered in the loop between residues 223‐235 (Photinus pyralis sequence) and 227, 228 and 229, indicating their involvement in labile interactions.
Luciferase from Fulgeochlizus bruchi (Coleoptera:Elateridae), a Brazilian click-beetle with a single abdominal lantern: molecular evolution, biological function and comparison with other click-beetle luciferases.
  • D. Amaral, R. Prado, V. Viviani
  • Biology
    Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
  • 2012
TLDR
The slow luminescence decay rate of F. bruchiLuciferase in vitro reaction could be an adaptation of this luciferase for the long and sustained in vivo luminescent display of the click-beetle during the courtship, and could be useful for in vivo intracellular imaging.
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