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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.)

Influence of the C-terminal domain on the bioluminescence activity and color determination in green and red emitting beetle luciferases and luciferase-like enzyme

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Author(s):
Bevilaqua, V. R. [1] ; Carvalho, Mariele C. [1] ; Pelentir, Gabriel F. [2] ; Tomazini, Atilio [3] ; Murakami, Mario [3] ; Viviani, Vadim R. [1, 2, 4]
Total Authors: 6
Affiliation:
[1] Fed Univ Sao Carlos UFSCar, Grad Program Evolut Genet & Mol Biol, Sao Carlos - Brazil
[2] Fed Univ Sao Carlos UFSCar, Dept Phys Chem & Math, Sorocaba - Brazil
[3] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Biorenewables Natl Lab LNBR, Campinas, SP - Brazil
[4] Fed Univ Sao Carlos UFSCar, Grad Program Biotechnol & Environm Monitoring, Rod. Joao Leme Santos, SP 264, Km 110, Sorocaba, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES; v. 20, n. 1 JAN 2021.
Web of Science Citations: 0
Abstract

Beetle luciferases catalyze the bioluminescent oxidation of D-luciferin, producing bioluminescence colors ranging from green to red, using two catalytic steps: adenylation of D-luciferin to produce D-luciferyl-adenylate and PPi, and oxidation of D-luciferyl-adenylate, yielding AMP, CO2, and excited oxyluciferin, the emitter. Luciferases and CoA-ligases display a similar fold, with a large N-terminal domain, and a small C-terminal domain which undergoes rotation, closing the active site and promoting both adenylation and oxidative reactions. The effect of C-terminal domain deletion was already investigated for Photinus pyralis firefly luciferase, resulting in a red-emitting mutant with severely impacted luminescence activity. However, the contribution of C-terminal in the bioluminescence activities and colors of other beetle luciferases and related ancestral luciferases were not investigated yet. Here we compared the effects of the C-terminal domain deletion on green-emitting luciferases of Pyrearinus termitilluminans (Pte) click beetle and Phrixothrix vivianii railroadworm, and on the red-emitting luciferase of Phrixothrix hirtus railroadworm and luciferase-like enzyme of Zophobas morio. In all cases, the domain deletion severely impacted the overall bioluminescence activities and, slightly less, the oxidative activities, and usually red-shifted the bioluminescence colors. The results support the involvement of the C-terminal in shielding the active site from the solvent during the light emitting step. However, in Pte luciferase, the deletion caused only a 10 nm red-shift, indicating a distinctive active site which remains more shielded, independently of the C `-terminal. Altogether, the results confirm the main contribution of the C-terminal for the catalysis of the adenylation reaction and for active site shielding during the light emitting step. (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