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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.)

Luciferase isozymes from the Brazilian Aspisoma lineatum (Lampyridae) firefly: origin of efficient pH-sensitive lantern luciferases from fat body pH-insensitive ancestors

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Mazumder, Zeaul H. [1] ; Sharma, Debdulal [1] ; Sengupta, Devashish [1] ; Mukherjee, Avinaba [2] ; Boruah, Jayanta Sarmah [1] ; Basu, Samita [3] ; Shukla, Pradeep Kumar [4] ; Jha, Tarun [5]
Total Authors: 8
[1] Assam Univ, Dept Chem, Silchar 788011, Assam - India
[2] Univ Calcutta, Charurhandra Coll, Dept Zool, Kolkata 700029 - India
[3] Saha Inst Nucl Phys, Chem Sci Div, Kolkata 700064 - India
[4] Assam Univ, Dept Phys, Silchar 788011, Assam - India
[5] Jadavpur Univ, Dept Pharmaceut Technol, Kolkata 700032 - India
Total Affiliations: 5
Document type: Journal article
Source: PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES; v. 19, n. 12, p. 1776-1789, DEC 1 2020.
Web of Science Citations: 0

Firefly luciferases usually emit green-yellow bioluminescence at physiological pH values. However, under acidic conditions, in the presence of heavy metals and, at high temperatures they emit red bioluminescence. To understand the structural origin of bioluminescence colors and pH-sensitivity, about 20 firefly luciferases have been cloned, sequenced and investigated. The proton and metal-binding site responsible for pH- and metal sensitivity in firefly luciferases was shown to involve the residues H310, E311 and E354 in firefly luciferases. However, it is still unclear how and why pH-sensitivity arose and evolved in firefly luciferases. Here, we cloned and characterized two novel luciferase cDNAs from the fat body and lanterns of the Brazilian firefly Aspisoma lineatum. The larval fat body isozyme (AL2) has 545 residues, and displays very slow luminescence kinetics and a pH-insensitive spectrum. The adult lantern isozyme (AL1) has 548 residues, displays flash-like kinetics and pH and metal sensitive bioluminescence spectra, and is at least 10 times catalytically more efficient than AL2. Thermostability and CD studies showed that AL2 is much more stable and rigid than the AL1 isozyme. Multialignment and modelling studies show that the E310Q substitution (E310 in AL2 and Q310 in AL1) may have been critical for the origin of pH-sensitivity in firefly luciferases. The results indicate that the lantern efficient flash-emitting pH-sensitive luciferases arose from less efficient glow-type pH-insensitive luciferases found in the fat body of ancestral larval fireflies by enzyme structure flexibilization and substitution at position 310. (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 type: Research Projects - Thematic Grants
FAPESP's process: 16/07312-6 - Structure and biological function of luciferase-like enzime of Arachnocampa luminosa lanterns (Diptera: Keroplatidae) and luminescent activity development by genetic engineering
Grantee:Mariele Cristina de Carvalho
Support type: Scholarships in Brazil - Doctorate (Direct)