Cargando…

The Cruciality of Single Amino Acid Replacement for the Spectral Tuning of Biliverdin-Binding Cyanobacteriochromes

Cyanobacteriochromes (CBCRs), which are known as linear tetrapyrrole-binding photoreceptors, to date can only be detected from cyanobacteria. They can perceive light only in a small unit, which is categorized into various lineages in correlation with their spectral and structural characteristics. Re...

Descripción completa

Detalles Bibliográficos
Autores principales: Fushimi, Keiji, Hoshino, Hiroki, Shinozaki-Narikawa, Naeko, Kuwasaki, Yuto, Miyake, Keita, Nakajima, Takahiro, Sato, Moritoshi, Kano, Fumi, Narikawa, Rei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7504144/
https://www.ncbi.nlm.nih.gov/pubmed/32872628
http://dx.doi.org/10.3390/ijms21176278
_version_ 1783584556771704832
author Fushimi, Keiji
Hoshino, Hiroki
Shinozaki-Narikawa, Naeko
Kuwasaki, Yuto
Miyake, Keita
Nakajima, Takahiro
Sato, Moritoshi
Kano, Fumi
Narikawa, Rei
author_facet Fushimi, Keiji
Hoshino, Hiroki
Shinozaki-Narikawa, Naeko
Kuwasaki, Yuto
Miyake, Keita
Nakajima, Takahiro
Sato, Moritoshi
Kano, Fumi
Narikawa, Rei
author_sort Fushimi, Keiji
collection PubMed
description Cyanobacteriochromes (CBCRs), which are known as linear tetrapyrrole-binding photoreceptors, to date can only be detected from cyanobacteria. They can perceive light only in a small unit, which is categorized into various lineages in correlation with their spectral and structural characteristics. Recently, we have succeeded in identifying specific molecules, which can incorporate mammalian intrinsic biliverdin (BV), from the expanded red/green (XRG) CBCR lineage and in converting BV-rejective molecules into BV-acceptable ones with the elucidation of the structural basis. Among the BV-acceptable molecules, AM1_1870g3_BV4 shows a spectral red-shift in comparison with other molecules, while NpF2164g5_BV4 does not show photoconversion but stably shows a near-infrared (NIR) fluorescence. In this study, we found that AM1_1870g3_BV4 had a specific Tyr residue near the d-ring of the chromophore, while others had a highly conserved Leu residue. The replacement of this Tyr residue with Leu in AM1_1870g3_BV4 resulted in a blue-shift of absorption peak. In contrast, reverse replacement in NpF2164g5_BV4 resulted in a red-shift of absorption and fluorescence peaks, which applies to fluorescence bio-imaging in mammalian cells. Notably, the same Tyr/Leu-dependent color-tuning is also observed for the CBCRs belonging to the other lineage, which indicates common molecular mechanisms.
format Online
Article
Text
id pubmed-7504144
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-75041442020-09-24 The Cruciality of Single Amino Acid Replacement for the Spectral Tuning of Biliverdin-Binding Cyanobacteriochromes Fushimi, Keiji Hoshino, Hiroki Shinozaki-Narikawa, Naeko Kuwasaki, Yuto Miyake, Keita Nakajima, Takahiro Sato, Moritoshi Kano, Fumi Narikawa, Rei Int J Mol Sci Article Cyanobacteriochromes (CBCRs), which are known as linear tetrapyrrole-binding photoreceptors, to date can only be detected from cyanobacteria. They can perceive light only in a small unit, which is categorized into various lineages in correlation with their spectral and structural characteristics. Recently, we have succeeded in identifying specific molecules, which can incorporate mammalian intrinsic biliverdin (BV), from the expanded red/green (XRG) CBCR lineage and in converting BV-rejective molecules into BV-acceptable ones with the elucidation of the structural basis. Among the BV-acceptable molecules, AM1_1870g3_BV4 shows a spectral red-shift in comparison with other molecules, while NpF2164g5_BV4 does not show photoconversion but stably shows a near-infrared (NIR) fluorescence. In this study, we found that AM1_1870g3_BV4 had a specific Tyr residue near the d-ring of the chromophore, while others had a highly conserved Leu residue. The replacement of this Tyr residue with Leu in AM1_1870g3_BV4 resulted in a blue-shift of absorption peak. In contrast, reverse replacement in NpF2164g5_BV4 resulted in a red-shift of absorption and fluorescence peaks, which applies to fluorescence bio-imaging in mammalian cells. Notably, the same Tyr/Leu-dependent color-tuning is also observed for the CBCRs belonging to the other lineage, which indicates common molecular mechanisms. MDPI 2020-08-30 /pmc/articles/PMC7504144/ /pubmed/32872628 http://dx.doi.org/10.3390/ijms21176278 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Fushimi, Keiji
Hoshino, Hiroki
Shinozaki-Narikawa, Naeko
Kuwasaki, Yuto
Miyake, Keita
Nakajima, Takahiro
Sato, Moritoshi
Kano, Fumi
Narikawa, Rei
The Cruciality of Single Amino Acid Replacement for the Spectral Tuning of Biliverdin-Binding Cyanobacteriochromes
title The Cruciality of Single Amino Acid Replacement for the Spectral Tuning of Biliverdin-Binding Cyanobacteriochromes
title_full The Cruciality of Single Amino Acid Replacement for the Spectral Tuning of Biliverdin-Binding Cyanobacteriochromes
title_fullStr The Cruciality of Single Amino Acid Replacement for the Spectral Tuning of Biliverdin-Binding Cyanobacteriochromes
title_full_unstemmed The Cruciality of Single Amino Acid Replacement for the Spectral Tuning of Biliverdin-Binding Cyanobacteriochromes
title_short The Cruciality of Single Amino Acid Replacement for the Spectral Tuning of Biliverdin-Binding Cyanobacteriochromes
title_sort cruciality of single amino acid replacement for the spectral tuning of biliverdin-binding cyanobacteriochromes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7504144/
https://www.ncbi.nlm.nih.gov/pubmed/32872628
http://dx.doi.org/10.3390/ijms21176278
work_keys_str_mv AT fushimikeiji thecrucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT hoshinohiroki thecrucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT shinozakinarikawanaeko thecrucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT kuwasakiyuto thecrucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT miyakekeita thecrucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT nakajimatakahiro thecrucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT satomoritoshi thecrucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT kanofumi thecrucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT narikawarei thecrucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT fushimikeiji crucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT hoshinohiroki crucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT shinozakinarikawanaeko crucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT kuwasakiyuto crucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT miyakekeita crucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT nakajimatakahiro crucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT satomoritoshi crucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT kanofumi crucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes
AT narikawarei crucialityofsingleaminoacidreplacementforthespectraltuningofbiliverdinbindingcyanobacteriochromes