Comparative evaluation of the stability of seven-transmembrane microbial rhodopsins to various physicochemical stimuli

Honda, Naoya; Tsukamoto, Takashi; Sudo, Yuki

doi:10.1016/j.cplett.2017.05.055

Cited by 3 publications

(2 citation statements)

References 26 publications

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“…The hydrophobicity of these proteins is related to protein stability, which is also related to the stability of Tara76 rhodopsin. It reported that the stability of SDS detergent was influenced by hydrophobicity ( Honda et al., 2017 ). In this study, it was also shown that the hydrophobicity of Tara76 rhodopsin contributes significantly to the protein stability, which is suggested by the above results.…”

Section: Discussionmentioning

confidence: 99%

Discovery of a microbial rhodopsin that is the most stable in extreme environments

et al. 2021

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Summary Microbial rhodopsin is a retinal protein that functions as an ion pump, channel, and sensory transducer, as well as a light sensor, as in biosensors and biochips. Tara76 rhodopsin is a typical proton-pumping rhodopsin that exhibits strong stability against extreme pH, detergent, temperature, salt stress, and dehydration stress and even under dual and triple conditions. Tara76 rhodopsin has a thermal stability approximately 20 times higher than that of thermal rhodopsin at 80°C and is even stable at 85°C. Tara76 rhodopsin is also stable at pH 0.02 to 13 and exhibits strong resistance in detergent, including Triton X-100 and SDS. We tested the current flow that electrical current flow across dried proteins on the paper at high temperatures using an electrode device, which was measured stably from 25°C up to 120°C. These properties suggest that this Tara76 rhodopsin is suitable for many applications in the fields of bioengineering and biotechnology.

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Section: Discussionmentioning

confidence: 99%

Discovery of a microbial rhodopsin that is the most stable in extreme environments

et al. 2021

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“…For these modifications, research on rhodopsins showing a variety of such properties (absorption maxima, efficiency, kinetics and stability) would be useful. As a representative example, we recently identified a few rhodopsins with extremely high thermal stability (Tsukamoto et al 2013;Honda et al 2017;Kanehara et al 2017) and solved one of their crystal structures (Tsukamoto et al 2016). Combining experimental results with molecular simulations, some regions responsible for the high stability were estimated, and we are planning to insert that region into thermally unstable rhodopsins, such as HsSRI, to make them more stable.…”

Section: Future Directionsmentioning

confidence: 99%

Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering

et al. 2017

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Technological progress has enabled the successful application of functional conversion to a variety of biological molecules, such as nucleotides and proteins. Such studies have revealed the functionally essential elements of these engineered molecules, which are difficult to characterize at the level of an individual molecule. The functional conversion of biological molecules has also provided a strategy for their rational and atomistic design. The engineered molecules can be used in studies to improve our understanding of their biological functions and to develop protein-based tools. In this review, we introduce the functional conversion of membrane-embedded photoreceptive retinylidene proteins (also called rhodopsins) and discuss these proteins mainly on the basis of results obtained from our own studies. This information provides insights into the molecular mechanism of light-induced protein functions and their use in optogenetics, a technology which involves the use of light to control biological activities.

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Molecular mechanism for thermal denaturation of thermophilic rhodopsin

2019

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Comparative evaluation of the stability of seven-transmembrane microbial rhodopsins to various physicochemical stimuli

Cited by 3 publications

References 26 publications

Discovery of a microbial rhodopsin that is the most stable in extreme environments

Discovery of a microbial rhodopsin that is the most stable in extreme environments

Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering

Molecular mechanism for thermal denaturation of thermophilic rhodopsin

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