The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophores
Abstract Isoforms of some ctenophore photoproteins show different maxima of bioluminescence spectra— the ones of mnemiopsin and bolinopsin have λmax at 490 and 500 nm, while λmax for velamin isoforms are at 500 and 508 nm. The reasons for the fact have not yet been established. Here we report on the...
Saved in:
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-08-01
|
| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-025-16796-7 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849226317249118208 |
|---|---|
| author | Ludmila P. Burakova Eugene S. Vysotski |
| author_facet | Ludmila P. Burakova Eugene S. Vysotski |
| author_sort | Ludmila P. Burakova |
| collection | DOAJ |
| description | Abstract Isoforms of some ctenophore photoproteins show different maxima of bioluminescence spectra— the ones of mnemiopsin and bolinopsin have λmax at 490 and 500 nm, while λmax for velamin isoforms are at 500 and 508 nm. The reasons for the fact have not yet been established. Here we report on the construction and characterization of a set of mutants of berovin from ctenophore Beroe abyssicola with a substitution of Ala in position 106, which was selected for mutagenesis based on the comparison of the amino acid sequences of ctenophore photoproteins and the spatial structure model of berovin, to the residues with different properties of their side chains. The appearance of only Ser in this position, and its OH group in particular, is demonstrated to result in a green light emission. Moreover, we propose a plausible mechanism of bioluminescence spectrum shift towards longer wavelengths and the function of certain residues situated near OH group of the 6-(p-hydroxy)-phenyl substituent of coelenterazine in this process. We also conclude that the suggested mechanism of emitter formation is valid for other ctenophore photoproteins as well. |
| format | Article |
| id | doaj-art-ecfdf12af433489dae099a806f2d0325 |
| institution | Kabale University |
| issn | 2045-2322 |
| language | English |
| publishDate | 2025-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj-art-ecfdf12af433489dae099a806f2d03252025-08-24T11:28:03ZengNature PortfolioScientific Reports2045-23222025-08-0115111110.1038/s41598-025-16796-7The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophoresLudmila P. Burakova0Eugene S. Vysotski1Photobiology Laboratory, Institute of Biophysics of Siberian Branch of the Russian Academy of Sciences, Federal Research Center “Krasnoyarsk Science Center” of Siberian Branch of the Russian Academy of SciencesPhotobiology Laboratory, Institute of Biophysics of Siberian Branch of the Russian Academy of Sciences, Federal Research Center “Krasnoyarsk Science Center” of Siberian Branch of the Russian Academy of SciencesAbstract Isoforms of some ctenophore photoproteins show different maxima of bioluminescence spectra— the ones of mnemiopsin and bolinopsin have λmax at 490 and 500 nm, while λmax for velamin isoforms are at 500 and 508 nm. The reasons for the fact have not yet been established. Here we report on the construction and characterization of a set of mutants of berovin from ctenophore Beroe abyssicola with a substitution of Ala in position 106, which was selected for mutagenesis based on the comparison of the amino acid sequences of ctenophore photoproteins and the spatial structure model of berovin, to the residues with different properties of their side chains. The appearance of only Ser in this position, and its OH group in particular, is demonstrated to result in a green light emission. Moreover, we propose a plausible mechanism of bioluminescence spectrum shift towards longer wavelengths and the function of certain residues situated near OH group of the 6-(p-hydroxy)-phenyl substituent of coelenterazine in this process. We also conclude that the suggested mechanism of emitter formation is valid for other ctenophore photoproteins as well.https://doi.org/10.1038/s41598-025-16796-7 |
| spellingShingle | Ludmila P. Burakova Eugene S. Vysotski The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophores Scientific Reports |
| title | The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophores |
| title_full | The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophores |
| title_fullStr | The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophores |
| title_full_unstemmed | The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophores |
| title_short | The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophores |
| title_sort | key residue responsible for the red shift of bioluminescence spectra of light sensitive ca2 regulated photoproteins of ctenophores |
| url | https://doi.org/10.1038/s41598-025-16796-7 |
| work_keys_str_mv | AT ludmilapburakova thekeyresidueresponsiblefortheredshiftofbioluminescencespectraoflightsensitiveca2regulatedphotoproteinsofctenophores AT eugenesvysotski thekeyresidueresponsiblefortheredshiftofbioluminescencespectraoflightsensitiveca2regulatedphotoproteinsofctenophores AT ludmilapburakova keyresidueresponsiblefortheredshiftofbioluminescencespectraoflightsensitiveca2regulatedphotoproteinsofctenophores AT eugenesvysotski keyresidueresponsiblefortheredshiftofbioluminescencespectraoflightsensitiveca2regulatedphotoproteinsofctenophores |