A novel photoprotein from oceanic squid (Symplectoteuthis oualaniensis) with sequence similarity to mammalian carbon–nitrogen hydrolase domains

Fujii, Tatsuya; Ahn, Jung-Youb; Kuse, Masaki; Mori, Hitoshi; Matsuda, Tsukasa; Isobe, Mitsuaki

doi:10.1016/s0006-291x(02)00296-6

Cited by 24 publications

(18 citation statements)

References 21 publications

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“…4) The 40 kDa fragment still had bioluminescent activity as well as fluorescence, suggesting that the presence of the bound luminous substance. We then analyzed the amino acid sequence of symplectin with Edman degradation, nano-LC-ESI-Q-TOF-MS and MS/MS analysis, 5) as well as cloning and sequencing of the cDNA.…”

Section: Resultsmentioning

confidence: 97%

Cysteine-390 is the binding site of luminous substance with symplectin, a photoprotein from Okinawan squid, Symplectoteuthis oualaniensis

Isobe

Kuse

Tani

et al. 2008

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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Symplectin is a photoprotein from a luminous squid, Symplectoteuthis oualaniensis. It has a luminous substrate, dehydrocoelenterazine (DCZ), linked through a thioether bond with a cysteine residue. We have proven the binding site of luminous substrate in symplectin by using an artificial analogue of DCZ, ortho-fluoro-DCZ (F-DCZ). F-DCZsymplectin emitting strong blue light was reconstituted from apo-symplectin and F-DCZ. Proteolytic digestion of the reconstituted F-DCZ-symplectin afforded peptides including C 390 GLK-F-DCZ (amide), which was detected with a house assembled nano-LC-ESI-Q-TOF-MS. The chromo-peptide derived from the F-DCZ-symplectin after luminescence showed the lower molecular mass than that before the luminescence by 12 mass units, corresponding to the loss of one carbon atom upon emitting light. Thus, we have concluded that F-DCZ analogue binds to Cys390 in symplectin so as to emit light.

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Section: Resultsmentioning

confidence: 97%

Cysteine-390 is the binding site of luminous substance with symplectin, a photoprotein from Okinawan squid, Symplectoteuthis oualaniensis

Isobe

Kuse

Tani

et al. 2008

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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“…Coelenterazine ( 7 ) could not restore the luminescence of this photoprotein, whereas dehydrocoelenterazine ( 20 ) or the corresponding dithiothreitol and glutathione adducts could 31. Further work led to purer samples of symplectin, which confirmed the originality of this photoprotein,32 and it could be reconstituted from aposymplectin and dehydrocoelenterazine ( 20 ) 33. Pholasin, a photoprotein isolated from the mollusk P. dactylus , was reported more recently to become three time more luminescent in the presence of added dehydrocoelenterazine ( 20 ) 34…”

Section: Introduction: Natural Bioluminescent Systems Involving Immentioning

confidence: 79%

Synthetic Routes to Coelenterazine and Other Imidazo[1,2‐a]pyrazin‐3‐one Luciferins: Essential Tools for Bioluminescence‐Based Investigations

Coutant

Janin

2015

Chemistry A European J

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In the last few decades, bioluminescent systems based on the expression of a luciferase and the addition of a luciferin to monitor the emission of light have become very important tools for biological investigations. A growing proportion of these systems use coelenterazine or analogues of imidazo[1,2-a]pyrazine luciferins along with photoproteins or luciferases from sea creatures such as Aequorea, Renilla, Gaussia or Oplophorus. Central to the success of these tools are the synthetic pathways developed not only to prepare the naturally occurring luciferins, but also to design altered compounds that exhibit improved bioluminescence. Current work is indeed focused on the design of systems exhibiting extended luminescence ("glow" systems) or redshifted wavelengths, as well as constructions better adapted to conditions in cells or in vivo. This review describes the synthetic pathways used to prepare imidazo[1,2-a]pyrazine luciferins along with the research efforts aimed at preparing analogues even better suited to the design of assays.

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“…Coelenterazine (7)c ould not restoret he luminescenceo ft his photoprotein, whereas dehydrocoelenterazine (20)o rt he corresponding dithiothreitol and glutathione adducts could. [31] Further work led to purer samples of symplectin,w hich confirmed the originality of this photoprotein, [32] and it could be reconstituted from aposymplectin and dehydrocoelenterazine (20). [33] Pholasin, ap hotoproteini solated from the mollusk P. dactylus, was reported more recently to become three time more luminescent in the presence of added dehydrocoelenterazine (20).…”

Section: Introduction:natural Bioluminescent Systems Involving Imidazmentioning

confidence: 84%

ChemInform Abstract: Synthetic Routes to Coelenterazine and Other Imidazo[1,2‐a]pyrazin‐3‐one Luciferins: Essential Tools for Bioluminescence‐Based Investigations

Coutant

Janin

2016

ChemInform

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A novel photoprotein from oceanic squid (Symplectoteuthis oualaniensis) with sequence similarity to mammalian carbon–nitrogen hydrolase domains

Cited by 24 publications

References 21 publications

Cysteine-390 is the binding site of luminous substance with symplectin, a photoprotein from Okinawan squid, Symplectoteuthis oualaniensis

Cysteine-390 is the binding site of luminous substance with symplectin, a photoprotein from Okinawan squid, Symplectoteuthis oualaniensis

Synthetic Routes to Coelenterazine and Other Imidazo[1,2‐a]pyrazin‐3‐one Luciferins: Essential Tools for Bioluminescence‐Based Investigations

ChemInform Abstract: Synthetic Routes to Coelenterazine and Other Imidazo[1,2‐a]pyrazin‐3‐one Luciferins: Essential Tools for Bioluminescence‐Based Investigations

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