Protein Engineering of Dual-Cys Cyanobacteriochrome AM1_1186g2 for Biliverdin Incorporation and Far-Red/Blue Reversible Photoconversion

Autor:	Moritoshi Sato, Takahiro Nakajima, Masahiko Ikeuchi, Rei Narikawa, Yuto Kuwasaki, Yoshibumi Ueda, Keita Miyake, Yuka Takeda, Keiji Fushimi
Rok vydání:	2019
Předmět:	0301 basic medicine Light bilin Cyanobacteria Photoreceptors Microbial Protein Engineering Photochemistry Article Catalysis lcsh:Chemistry Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound Phycocyanobilin Amino Acid Sequence Physical and Theoretical Chemistry lcsh:QH301-705.5 Molecular Biology Spectroscopy reversible Cys adduct formation Biliverdin Molecular Structure 030102 biochemistry & molecular biology Phytochrome Protein Stability Chemistry Biliverdine Organic Chemistry Far-red General Medicine Chromophore Tetrapyrrole Computer Science Applications 030104 developmental biology Dark state lcsh:Biology (General) lcsh:QD1-999 Cyanobacteriochrome site-directed mutagenesis
Zdroj:	International Journal of Molecular Sciences Volume 20 Issue 12 International Journal of Molecular Sciences, Vol 20, Iss 12, p 2935 (2019)
ISSN:	1422-0067
Popis:	Cyanobacteria have cyanobacteriochromes (CBCRs), which are photoreceptors that bind to a linear tetrapyrrole chromophore and sense UV-to-visible light. A recent study revealed that the dual-Cys CBCR AM1_1186g2 covalently attaches to phycocyanobilin and exhibits unique photoconversion between a Pr form (red-absorbing dark state, &lambda max = 641 nm) and Pb form (blue-absorbing photoproduct, &lambda max = 416 nm). This wavelength separation is larger than those of the other CBCRs, which is advantageous for optical tools. Nowadays, bioimaging and optogenetics technologies are powerful tools for biological research. In particular, the utilization of far-red and near-infrared light sources is required for noninvasive applications to mammals because of their high potential to penetrate into deep tissues. Biliverdin (BV) is an intrinsic chromophore and absorbs the longest wavelength among natural linear tetrapyrrole chromophores. Although the BV-binding photoreceptors are promising platforms for developing optical tools, AM1_1186g2 cannot efficiently attach BV. Herein, by rationally introducing several replacements, we developed a BV-binding AM1_1186g2 variant, KCAP_QV, that exhibited reversible photoconversion between a Pfr form (far-red-absorbing dark state, &lambda max = 691 nm) and Pb form (&lambda max = 398 nm). This wavelength separation reached 293 nm, which is the largest among the known phytochrome and CBCR photoreceptors. In conclusion, the KCAP_QV molecule developed in this study can offer an alternative platform for the development of unique optical tools.
Databáze:	OpenAIRE
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