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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

A new brilliantly blue-emitting luciferin-luciferase system from Orfelia fultoni and Keroplatinae (Diptera)

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Author(s):
Viviani, Vadim R. [1, 2] ; Silva, Jaqueline R. [1] ; Amaral, Danilo T. [1] ; Bevilaqua, Vanessa R. [2] ; Abdalla, Fabio C. [1] ; Branchini, Bruce R. [3] ; Johnson, Carl H. [4]
Total Authors: 7
Affiliation:
[1] Fed Univ Sao Carlos UFSCar, Grad Sch Biotechnol & Environm Monitoring UFSCar, Sorocaba - Brazil
[2] Grad Sch Evolut Genet & Mol Biol UFSCar, Sao Carlos - Brazil
[3] Connecticut Coll, Dept Chem, New London, CT 06320 - USA
[4] Vanderbilt Univ, Dept Biol Sci, 221 Kirkland Hall, Nashville, TN 37235 - USA
Total Affiliations: 4
Document type: Journal article
Source: SCIENTIFIC REPORTS; v. 10, n. 1 JUN 15 2020.
Web of Science Citations: 0
Abstract

Larvae of O. fultoni (Keroplatidae: Keroplatinae), which occur along river banks in the Appalachian Mountains in Eastern United States, produce the bluest bioluminescence among insects from translucent areas associated to black bodies, which are located mainly in the anterior and posterior parts of the body. Although closely related to Arachnocampa spp (Keroplatidae: Arachnocampininae), O.fultoni has a morphologically and biochemically distinct bioluminescent system which evolved independently, requiring a luciferase enzyme, a luciferin, a substrate binding fraction (SBF) that releases luciferin in the presence of mild reducing agents, molecular oxygen, and no additional cofactors. Similarly, the closely related Neoceroplatus spp, shares the same kind of luciferin-luciferase system of Orfelia fultoni. However, the molecular properties, identities and functions of luciferases, SBF and luciferin of Orfelia fultoni and other luminescent members of the Keroplatinae subfamily still remain to be fully elucidated. Using O. fultoni as a source of luciferase, and the recently discovered non-luminescent cave worm Neoditomiya sp as the main source of luciferin and SBF, we isolated and initially characterized these compounds. The luciferase of O. fultoni is a stable enzyme active as an apparent trimer (220kDa) composed of similar to 70kDa monomers, with an optimum pH of 7.8. The SBF, which is found in the black bodies in Orfelia fultoni and in smaller dark granules in Neoditomiya sp, consists of a high molecular weight complex of luciferin and proteins, apparently associated to mitochondria. The luciferin, partially purified from hot extracts by a combination of anion exchange chromatography and TLC, is a very polar and weakly fluorescent compound, whereas its oxidized product displays blue fluorescence with an emission spectrum matching the bioluminescence spectrum (similar to 460nm), indicating that it is oxyluciferin. The widespread occurrence of luciferin and SBF in both luminescent and non-luminescent Keroplatinae larvae indicate an additional important biological function for the substrate, and therefore the name keroplatin. (AU)

FAPESP's process: 10/05426-8 - Arthropod bioluminescence: biological diversity in Brazilian biomes, biochemical origin, structural/functional evolution of luciferases, molecular differentiation of lanterns, biotechnological, environmental and educational applications
Grantee:Vadim Viviani
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 14/50583-5 - Identification of the luciferases and acessory proteins of the bioluminescent system of Orfelia fultonii (Diptera : Keroplatidae): transcriptional and proteomic analysis
Grantee:Vadim Viviani
Support Opportunities: Regular Research Grants