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  NeoR, a near-infrared absorbing rhodopsin

Broser, M., Spreen, A., Konold, P. E., Peter, E., Adam, S., Borin, V., et al. (2020). NeoR, a near-infrared absorbing rhodopsin. Nature Communications, 11: 5682. doi:10.1038/s41467-020-19375-8.

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s41467-020-19375-8.pdf (Verlagsversion), 3MB
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 Urheber:
Broser, Matthias1, Autor
Spreen, Anika1, Autor
Konold, Patrick E1, Autor
Peter, Enrico1, Autor
Adam, Suliman1, Autor
Borin, Veniamin1, Autor
Schapiro, Igor1, Autor
Seifert, Reinhard2, Autor           
Kennis, John T M1, Autor
Bernal Sierra, Yinth Andrea1, Autor
Hegemann, Peter1, Autor
Affiliations:
1External Organizations, ou_persistent22              
2Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society, ou_2173679              

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 Zusammenfassung: The "Rhizoclosmatium globosum" genome encodes three rhodopsin-guanylyl cyclases (RGCs), which are predicted to facilitate visual orientation of the fungal zoospores. Here, we show that RGC1 and RGC2 function as light-activated cyclases only upon heterodimerization with RGC3 (NeoR). RGC1/2 utilize conventional green or blue-light-sensitive rhodopsins (λmax = 550 and 480 nm, respectively), with short-lived signaling states, responsible for light-activation of the enzyme. The bistable NeoR is photoswitchable between a near-infrared-sensitive (NIR, λmax = 690 nm) highly fluorescent state (QF = 0.2) and a UV-sensitive non-fluorescent state, thereby modulating the activity by NIR pre-illumination. No other rhodopsin has been reported so far to be functional as a heterooligomer, or as having such a long wavelength absorption or high fluorescence yield. Site-specific mutagenesis and hybrid quantum mechanics/molecular mechanics simulations support the idea that the unusual photochemical properties result from the rigidity of the retinal chromophore and a unique counterion triad composed of two glutamic and one aspartic acids. These findings substantially expand our understanding of the natural potential and limitations of spectral tuning in rhodopsin photoreceptors.

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Sprache(n): eng - English
 Datum: 2020-11-10
 Publikationsstatus: Online veröffentlicht
 Seiten: 10
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 33173168
DOI: 10.1038/s41467-020-19375-8
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Titel: Nature Communications
  Kurztitel : Nat Commun
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: London : Nature Publishing Group
Seiten: - Band / Heft: 11 Artikelnummer: 5682 Start- / Endseite: - Identifikator: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723