A unique photochromic UV-A sensor protein Rc-PYP interacting with PYP-binding protein

2021 ◽  
Author(s):  
Suhyang Kim ◽  
Yusuke Nakasone ◽  
Akira Takakado ◽  
Yoichi Yamazaki ◽  
Hironari Kamikubo ◽  
...  
Keyword(s):  
Binding Protein ◽  
Photoactive Yellow Protein ◽  
Partner Protein ◽  
Light Sensor ◽  
Sensor Protein ◽  
Sensor Proteins

Photoactive yellow protein (PYP) is one of typical light sensor proteins. Although its photoreaction has been extensively studied, no downstream partner protein has been identified to date. In this study,...

Photoinduced dimerization of a photosensory DNA-binding protein EL222 and its LOV domain

2017 ◽  
Vol 19 (36) ◽  
pp. 24855-24865 ◽  
Author(s):  
Akira Takakado ◽  
Yusuke Nakasone ◽  
Masahide Terazima
Keyword(s):  
Dna Binding ◽  
Binding Affinity ◽  
Blue Light ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Lov Domain ◽  
Light Sensor ◽  
Target Dna ◽  
Sensor Protein ◽  
Dna Binding Affinity

Blue light sensor protein EL222, which regulates DNA-binding affinity, exhibits photoinduced dimerization in the absence of target DNA.

scholarly journals Interaction of a photochromic UV sensor protein Rc-PYP with PYP-binding protein

2021 ◽  
Author(s):  
Suhyang Kim ◽  
Yusuke Nakasone ◽  
Akira Takakado ◽  
Yoichi Yamazaki ◽  
Hironari Kamikubo ◽  
...  
Keyword(s):  
Rhodobacter Capsulatus ◽  
Transient Absorption ◽  
Uv Light ◽  
Binding Protein ◽  
Reaction Scheme ◽  
Complex Ii ◽  
Uv Sensor ◽  
Light Sensor ◽  
Halorhodospira Halophila ◽  
Sensor Proteins

Photoactive yellow protein (PYP) from Halorhodospira halophila is one of typical light sensor proteins. Although its photoreaction has been extensively studied, no downstream partner protein has been identified to date. In this study, the intermolecular interaction dynamics observed between PYP from Rhodobacter capsulatus (Rc-PYP) and a possible downstream protein, PYP-binding protein (PBP), were studied. It was found that UV light-induced a long-lived product (pUV*), which interacts with PBP to form a stable hetero-hexamer (Complex-Ⅱ). The reaction scheme for this interaction was revealed using transient absorption and transient grating methods. Time-resolved diffusion detection showed that a hetero-trimer (Complex-Ⅰ) is formed transiently, which produced Complex-II via a second-order reaction. Any other intermediates, including those from pBL do not interact with PBP. The reaction scheme and kinetics are determined. Interestingly, long-lived Complex-II dissociates upon excitation with blue light. These results demonstrate that Rc-PYP is a photochromic and new type of UV sensor, of which signaling process is similar to that of other light sensor proteins in the visible light region. The photochromic heterogeneous intermolecular interactions formed between PYP and PBP can be used as a novel and useful tool in optogenetics.

Anomalous pressure effects on the photoreaction of a light-sensor protein from Synechocystis, PixD (Slr1694), and the compressibility change of its intermediates

2016 ◽  
Vol 18 (37) ◽  
pp. 25915-25925 ◽  
Author(s):  
Tsubasa Nakajima ◽  
Kunisato Kuroi ◽  
Yusuke Nakasone ◽  
Koji Okajima ◽  
Masahiko Ikeuchi ◽  
...  
Keyword(s):  
High Pressure ◽  
Pressure Effect ◽  
Pressure Effects ◽  
Light Sensor ◽  
Sensor Protein

High pressure enhances the dissociation yield of SyPixD, and this pressure effect was explained by pressure dependent fluctuation of intermediates.

scholarly journals 3P269 FTIR analysis of the photoreactions of red/green light sensor protein AnPixJ(Photobiology: Vision & Photoreception,The 48th Annual Meeting of the Biophysical Society of Japan)

2010 ◽  
Vol 50 (supplement2) ◽  
pp. S192-S193
Author(s):  
Yusuke Tomita ◽  
Hiroyuki Suzuki ◽  
Rei Narikawa ◽  
Masahiko Ikeuchi ◽  
Shigeru Itoh ◽  
...  
Keyword(s):  
Annual Meeting ◽  
Green Light ◽  
Ftir Analysis ◽  
Light Sensor ◽  
Sensor Protein ◽  
Biophysical Society
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