A Proteorhodopsin-Related Photosensor Expands the Repertoire of Structural Motifs Employed by Sensory Rhodopsins.


Journal

The journal of physical chemistry. B
ISSN: 1520-5207
Titre abrégé: J Phys Chem B
Pays: United States
ID NLM: 101157530

Informations de publication

Date de publication:
21 09 2023
Historique:
pmc-release: 11 09 2024
medline: 22 9 2023
pubmed: 11 9 2023
entrez: 11 9 2023
Statut: ppublish

Résumé

Microbial rhodopsins are light-activated retinal-binding membrane proteins that perform a variety of ion transport and photosensory functions. They display several cases of convergent evolution where the same function is present in unrelated or very distant protein groups. Here we report another possible case of such convergent evolution, describing the biophysical properties of a new group of sensory rhodopsins. The first representative of this group was identified in 2004 but none of the members had been expressed and characterized. The well-studied haloarchaeal sensory rhodopsins interacting with methyl-accepting Htr transducers are close relatives of the halobacterial proton pump bacteriorhodopsin. In contrast, the sensory rhodopsins we describe here are relatives of proteobacterial proton pumps, proteorhodopsins, but appear to interact with Htr-like transducers likewise, even though they do not conserve the residues important for the interaction of haloarchaeal sensory rhodopsins with their transducers. The new sensory rhodopsins display many unusual amino acid residues, including those around the retinal chromophore; most strikingly, a tyrosine in place of a carboxyl counterion of the retinal Schiff base on helix C. To characterize their unique sequence motifs, we augment the spectroscopy and biochemistry data by structural modeling of the wild-type and three mutants. Taken together, the experimental data, bioinformatics sequence analyses, and structural modeling suggest that the tyrosine/aspartate complex counterion contributes to a complex water-mediated hydrogen-bonding network that couples the protonated retinal Schiff base to an extracellular carboxylic dyad.

Identifiants

pubmed: 37694950
doi: 10.1021/acs.jpcb.3c04032
pmc: PMC10519204
doi:

Substances chimiques

proteorhodopsin 0
Sensory Rhodopsins 0
Schiff Bases 0
Rhodopsins, Microbial 0
Bacteriorhodopsins 53026-44-1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

7872-7886

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Auteurs

Maryam Saliminasab (M)

Department of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario N1G 2W1, Canada.

Yoichi Yamazaki (Y)

Division of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.

Alyssa Palmateer (A)

Department of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario N1G 2W1, Canada.

Andrew Harris (A)

Department of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario N1G 2W1, Canada.

Luiz Schubert (L)

Experimental Molecular Biophysics Group, Department of Physics, Freie Universität Berlin, D-14195 Berlin, Germany.

Pit Langner (P)

Experimental Molecular Biophysics Group, Department of Physics, Freie Universität Berlin, D-14195 Berlin, Germany.

Joachim Heberle (J)

Experimental Molecular Biophysics Group, Department of Physics, Freie Universität Berlin, D-14195 Berlin, Germany.

Ana-Nicoleta Bondar (AN)

University of Bucharest, Faculty of Physics, Atomiştilor 405, Măgurele 077125, Romania.
Forschungszentrum Jülich, Institute for Neuroscience and Medicine and Institute for Advanced Simulations (IAS-5/INM-9), Computational Biomedicine, Wilhelm-Johnen Straße, 52428 Jülich, Germany.

Leonid S Brown (LS)

Department of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario N1G 2W1, Canada.

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