Genomic structure of the luciferase gene and phylogenetic analysis in the Hotaria-group fireflies

Choi, Yong Soo; Bae, Jin Sik; Lee, Kwang-Sik; Kim, Seong Ryul; Kim, Iksoo; Kim, Jong Gill; Kim, Keun Young; Kim, Sam Eun; Suzuki, Hirobumi; Lee, Sang Mong; Sohn, Hung Dae; Jin, Byung Rae

doi:10.1016/s1096-4959(02)00249-x

Cited by 18 publications

(14 citation statements)

References 20 publications

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“…were readily cloned, sequenced, and characterized ( Table 1). All luciferases are a single polypeptide chain and show high sequence identities among them with 48-99% identity [125,126].…”

Section: Primary Structure Of Firefly Luciferasementioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

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Firefly luciferase is a member of the acyl-adenylate/thioester-forming superfamily of enzymes and catalyzes the oxidation of firefly luciferin with molecular oxygen to emit light. Knowledge of the luminescence mechanism catalyzed by firefly luciferase has been gathered, leading to the discovery of a novel catalytic function of luciferase. Recently, we demonstrated that firefly luciferase has a catalytic function of fatty acyl-CoA synthesis from fatty acids in the presence of ATP, Mg(2+) and coenzyme A. Based on identification of fatty acyl-CoA genes in firefly, Drosophila, and non-luminous click beetles, we then proposed that the evolutionary origin of firefly luciferase is a fatty acyl-CoA synthetase in insects. Further, we succeeded in converting the fatty acyl-CoA synthetase of non-luminous insects into functional luciferase showing luminescence activity by site-directed mutagenesis.

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“…were readily cloned, sequenced, and characterized ( Table 1). All luciferases are a single polypeptide chain and show high sequence identities among them with 48-99% identity [125,126].…”

Section: Primary Structure Of Firefly Luciferasementioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

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“…The previous studies on luciferase genes of L. lateralis also indicate they are all the same length (Tatsumi et al, 1992;Cho et al, 1999). This feature is conserved among species of the Luciolinae subfamily (Masuda et al, 1989;Devine et al, 1993;Choi et al, 2002Choi et al, , 2003. The analysis of the exon/intron boundary suggested the presence of seven exons in the luciferase gene of L. lateralis.…”

Section: Discussionmentioning

confidence: 73%

“…More than 10 luciferase genes have been isolated from various firefly species. These include several species of the Luciolagroup such as L. lateralis (Tatsumi et al, 1992;Cho et al, 1999), L. cruciata (Masuda et al, 1989) and L. mingrelica (Devine et al, 1993) and the Hotaria-group such as H. parvula (Ohmiya et al, 1995), H. unmunsana (Choi et al, 2002), H. papariensis (Choi et al, 2003), and H. tsushimana (Choi et al, 2003). Ye et al (1997) cloned and sequenced the luciferase from Photuris pennsylvanica of the Photurinae subfamily of the Lampyridae and compared it to that of several Luciolinae and one species of Hotaria.…”

Section: Introductionmentioning

confidence: 99%

Genomic structure and phylogenetic analysis of the luciferase gene of the firefly, Luciola lateralis (Coleoptera: Lampyridae)

Kim¹,

Choi²,

Kim³

et al. 2004

Eur. J. Entomol.

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The complete nucleotide sequence and the exon-intron structure of the luciferase gene of the firefly, Luciola lateralis (Coleoptera: Lampyridae) is described. The luciferase gene of the L. lateralis firefly spans 1,971 bp and consists of six introns and seven exons coding for 548 amino acid residues. From samples collected at Boun and Muju, Korea, three isoforms, with identical exon-intron structure, named BU, MJ1 and MJ2, respectively, were obtained. Although the amino acid sequences of MJ1 and MJ2 were identical to those of known luciferase genes of Korean origin, the BU type was novel, differing from each of the MJ1 and MJ2 types by one amino acid. The luciferase sequences of the Korean samples, including those previously revealed, differed only by one-two amino acid residues, but differed by five-six amino acid residues from that of the luciferase gene recorded from specimens from Japan, which suggest genetic divergence has occurred in this species. Phylogenetic analyses using both amino acid and nucleotide sequences further showed that the luciferase gene of the Japanese L. lateralis firefly is genetically distinguishable from that of Korean L. lateralis, suggesting the presence of a genetic subdivision between the L. lateralis dwelling in the Korean Peninsula and Japanese Islands.

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“…The conversion of long chain fatty acids to fatty acyl-CoA is the initial and essential step in fatty acids metabolism [38]. Whereas the amino acid sequences of the reported luciferases among Asiatic fireflies are highly similar (80.8–90%) [39], it is likely that the unexplored luciferase of L. cerata also retains a similar catalytic activity to long chain fatty acids. These evidences suggested that the lcFABP might play a key role in supplying long chain fatty acids to peroxisomes for the luciferase-catalyzed long chain fatty acyl-CoA synthetic reaction in photocytes.…”

Section: Discussionmentioning

confidence: 99%

A Photocytes-Associated Fatty Acid-Binding Protein from the Light Organ of Adult Taiwanese Firefly, Luciola cerata

Goh

2011

PLoS ONE

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BackgroundIntracellular fatty acid-binding proteins (FABPs) are considered to be an important energy source supplier in lipid metabolism; however, they have never been reported in any bioluminescent tissue before. In this study, we determined the structural and functional characteristics of a novel FABP (lcFABP) from the light organ of adult Taiwanese firefly, Luciola cerata, and showed anatomical association of lcFABP with photocytes.Principal FindingsOur results demonstrated the primary structure of lcFABP deduced from the cDNA clone of light organ shares structural homologies with other insect and human FABPs. In vitro binding assay indicated the recombinant lcFABP binds saturated long chain fatty acids (C14-C18) more strongly than other fatty acids and firefly luciferin. In addition, tissue distribution screening assay using a rabbit antiserum specifically against the N-terminal sequence of lcFABP confirmed the light organ-specific expression of lcFABP. In the light organ, the lcFABP constituted about 15% of total soluble proteins, and was detected in both cytosol and nucleus of photocytes.ConclusionsThe specific localization of abundant lcFABP in the light organ suggests that sustained bioluminescent flashes in the light organ might be a high energy demanding process. In photocytes, lcFABP might play a key role in providing long chain fatty acids to peroxisomes for the luciferase-catalyzed long chain acyl-CoA synthetic reaction.

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Genomic structure of the luciferase gene and phylogenetic analysis in the Hotaria-group fireflies

Cited by 18 publications

References 20 publications

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Genomic structure and phylogenetic analysis of the luciferase gene of the firefly, Luciola lateralis (Coleoptera: Lampyridae)

A Photocytes-Associated Fatty Acid-Binding Protein from the Light Organ of Adult Taiwanese Firefly, Luciola cerata

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