Signal relay from sensory rhodopsin I to the cognate transducer HtrI: Assessing the critical change in hydrogen-bonding between Tyr-210 and Asn-53

Radu, Ionela; Budyak, Ivan L.; Hoomann, Torben; Kim, Young Jun; Engelhard, Martin; Labahn, Jörg; Büldt, Georg; Heberle, Joachim; Schlesinger, Ramona

doi:10.1016/j.bpc.2010.02.017

Cited by 3 publications

(4 citation statements)

References 31 publications

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“…The new gene has been cloned under the control of the T7 promoter in pET15b (Amp r ; Invitrogen AG, Carlsbad, CA, USA), expressed in Escherichia coli BL21-CodonPlus (DE3) RP (Invitrogen) and purified essentially as described in. 38 Surface-Tethering of Sensory Rhodopsin II and Light-Induced Difference SEIRAS. MACH-NpSRII is specifically bound to the gold surface via the terminal sulfhydryl group of the introduced cysteine residue.…”

Section: Methodsmentioning

confidence: 99%

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Disc Antenna Enhanced Infrared Spectroscopy: From Self-Assembled Monolayers to Membrane Proteins

et al. 2018

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Plasmonic surfaces have emerged as a powerful platform for biomolecular sensing applications and can be designed to optimize the plasmonic resonance for probing molecular vibrations at utmost sensitivity. Here, we present a facile procedure to generate metallic microdisc antenna arrays that are employed in surface-enhanced infrared absorption (SEIRA) spectroscopy of biomolecules. Transmission electron microscopy (TEM) grids are used as shadow mask deployed during physical vapor deposition of gold. The resulting disc-shaped antennas exhibit enhancement factors of the vibrational bands of 4 × 10 giving rise to a detection limit <1 femtomol (10 mol) of molecules. Surface-bound monolayers of 4-mercaptobenzoic acid show polyelectrolyte behavior when titrated with cations in the aqueous medium. Conformational rigidity of the self-assembled monolayer is validated by density functional theory calculations. The membrane protein sensory rhodopsin II is tethered to the disc antenna arrays and is fully functional as inferred from the light-induced SEIRA difference spectra. As an advance to previous studies, the accessible frequency range is improved and extended into the fingerprint region.

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Section: Methodsmentioning

confidence: 99%

“…Thus, the resulting MACH-NpSRII protein has the flanking sequences: MACHMVGLTTLF...HHHHHHHHHH. The new gene has been cloned under the control of the T7 promoter in pET15b (Amp r ; Invitrogen AG, Carlsbad, CA), expressed in Escherichia coli BL21-CodonPlus (DE3) RP (Invitrogen) and purified essentially as described in ref 38.…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

Disc Antenna Enhanced Infrared Spectroscopy: From Self-Assembled Monolayers to Membrane Proteins

et al. 2018

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“…One can see several residues known to be involved in the extensive hydrogen-bonding in PRs conserved in Proteo-SRs (Figure S1). For example, a homologue of GPR’s Glu142 (BR’s Ala126) in helix D is conserved, as are two asparagines in helix G, one of which precedes the retinal-binding lysine. − On the other hand, the residues known to be important for haloarchaeal SRs signaling (homologues of Thr189, Tyr199, and Thr204 of N. pharaonis SRII, and Tyr210 of H. salinarum SRI) are not conserved in Proteo-SRs. They also lack the aromatic Tyr/Phe signature in place of the cytoplasmic proton donor (Asp96 of BR) typical for all classical SRs, replacing it with methionine.…”

Section: Resultsmentioning

confidence: 99%

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

Saliminasab,

Yamazaki,

Palmateer

et al. 2023

J. Phys. Chem. B

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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.

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“…The strategy for cloning, expression and purification of the full‐length fusion protein Hs SRI ‐ HtrI is essentially the same as for the already described version Hs SRI‐HtrI 1–52 . A shortened sopI gene from H. salinarum , which lacks downstream sequences for the last 15 amino acids, was fused upstream of the full‐length Hs HtrI gene using the megaprimer PCR method .…”

Section: Methodsmentioning

confidence: 99%

Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers

Orekhov

Bothe

Steinhoff

et al. 2017

Photochem & Photobiology

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Archaeal photoreceptors consist of sensory rhodopsins in complex with their cognate transducers. After light excitation, a two-component signaling chain is activated, which is homologous to the chemotactic signaling cascades in enterobacteria. The latter system has been studied in detail. From structural and functional studies, a picture emerges which includes stable signaling complexes, which assemble to receptor arrays displaying hexagonal structural elements. At this higher order structural level, signal amplification and sensory adaptation occur. Here, we describe electron microscopy data, which show that also the archaeal phototaxis receptors sensory rhodopsin I and II in complex with their cognate transducers can form hexagonal lattices even in the presence of a detergent. This result could be confirmed by molecular dynamics calculations, which revealed similar structural elements. Calculations of the global modes of motion displayed one mode, which resembles the "U"-"V" transition of the NpSRII:NpHtrII complex, which was previously argued to represent a functionally relevant global conformational change accompanying the activation process [Ishchenko et al. (2013) J. Photochem. Photobiol. B 123, 55-58]. A model of cooperativity at the transmembrane level is discussed.

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Signal relay from sensory rhodopsin I to the cognate transducer HtrI: Assessing the critical change in hydrogen-bonding between Tyr-210 and Asn-53

Cited by 3 publications

References 31 publications

Disc Antenna Enhanced Infrared Spectroscopy: From Self-Assembled Monolayers to Membrane Proteins

Disc Antenna Enhanced Infrared Spectroscopy: From Self-Assembled Monolayers to Membrane Proteins

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

Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers

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