Effects of Solubilization on the Structure and Function of the Sensory Rhodopsin II/Transducer Complex

Klare, Johann P.; Bordignon, Enrica; Doebber, Meike; Fitter, Jörg; Kriegsmann, Jana; Chizhov, Igor; Steinhoff, Heinz‐Jürgen; Engelhard, Martin

doi:10.1016/j.jmb.2005.12.015

Cited by 46 publications

(43 citation statements)

References 65 publications

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“…3a). The absence of spectral broadening in the DDM-solubilized sample shows that SRIIHtrII 157 is monomerized in the detergent as reported previously (25). On the other hand, the proteoliposome and nanodisc samples exhibit marked broadening in their spectral shapes when compared with the detergent-solubilized sample, demonstrating the presence of parallel dimerization for these two samples.…”

Section: Nanodisc-inserted Srii-htrii Complex Is a Proper Model Forsupporting

confidence: 83%

HAMP Domain Signal Relay Mechanism in a Sensory Rhodopsin-Transducer Complex

Wang

Sasaki

Tsai

et al. 2012

Journal of Biological Chemistry

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Background: HAMP domains are four-helix bundles that transmit signals from receptor to output domains in signaling proteins/complexes. Results: Opposite stimulus-induced helix motions with opposite signal output are resolved for two tandem HAMP domains on a phototaxis transducer. Conclusion: A molecular mechanism for HAMP domain switching and signal transmission is proposed. Significance: The HAMP switching and relay mechanism is important to many signal transduction proteins.

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Section: Nanodisc-inserted Srii-htrii Complex Is a Proper Model Forsupporting

confidence: 83%

HAMP Domain Signal Relay Mechanism in a Sensory Rhodopsin-Transducer Complex

Wang

Sasaki

Tsai

et al. 2012

Journal of Biological Chemistry

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“…The first modification was the addition of a flexible linker of 11 residues connecting the cytoplasmic C terminus of BR and cytoplasmic N terminus of HtrII to ensure a 1:1 stoichiometry, as exists in the SRII-HtrII complex (24)(25)(26). The fusion of SRII and HtrII by their cytoplasmic ends in this manner permits normal phototaxis responses, indicating the linker does not influence signaling (see Fig.…”

Section: Resultsmentioning

confidence: 99%

Three strategically placed hydrogen-bonding residues convert a proton pump into a sensory receptor

Sudo

Spudich

2006

Proc. Natl. Acad. Sci. U.S.A.

102

125

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In haloarchaea, light-driven ion transporters have been modified by evolution to produce sensory receptors that relay light signals to transducer proteins controlling motility behavior. The proton pump bacteriorhodopsin and the phototaxis receptor sensory rhodopsin II (SRII) differ by 74% of their residues, with nearly all conserved residues within the photoreactive retinal-binding pocket in the membrane-embedded center of the proteins. Here, we show that three residues in bacteriorhodopsin replaced by the corresponding residues in SRII enable bacteriorhodopsin to efficiently relay the retinal photoisomerization signal to the SRII integral membrane transducer (HtrII) and induce robust phototaxis responses. A single replacement (Ala-215-Thr), bridging the retinal and the membrane-embedded surface, confers weak phototaxis signaling activity, and the additional two (surface substitutions Pro-200 -Thr and Val-210 -Tyr), expected to align bacteriorhodopsin and HtrII in similar juxtaposition as SRII and HtrII, greatly enhance the signaling. In SRII, the three residues form a chain of hydrogen bonds from the retinal's photoisomerized C13AC14 double bond to residues in the membrane-embedded ␣-helices of HtrII. The results suggest a chemical mechanism for signaling that entails initial storage of energy of photoisomerization in SRII's hydrogen bond between Tyr-174, which is in contact with the retinal, and Thr-204, which borders residues on the SRII surface in contact with HtrII, followed by transfer of this chemical energy to drive structural transitions in the transducer helices. The results demonstrate that evolution accomplished an elegant but simple conversion: The essential differences between transport and signaling proteins in the rhodopsin family are far less than previously imagined.bacteriorhodopsin ͉ phototaxis ͉ retinal ͉ sensory rhodopsin ͉ transport M icrobial rhodopsins are photochemically reactive membrane-embedded proteins with seven transmembrane ␣-helices that form a pocket for the chromophore retinal. They are widespread in the microbial world in prokaryotes (bacteria and archaea) and in eukaryotes (fungi and algae) (1-3). A striking characteristic of these photoactive proteins is their wide range of seemingly dissimilar functions. Some are light-driven transporters, such as the proton pumps bacteriorhodopsin (BR) in haloarchaea (4) and proteorhodopsin in marine bacteria (5). Others are light sensors, such as the phototaxis receptors sensory rhodopsins (SR) I and II in haloarchaea (6-8). These sensory rhodopsins relay signals by protein-protein interaction to SR integral membrane transducer proteins (Htr) I and II, respectively. The signal relay mechanism from SR receptors to their cognate Htr transducers has become a focus of interest in part because of its importance to the general understanding of communication between integral membrane proteins, about which little is known.A close relationship between transport and sensory signaling activities was revealed when SRI was separated from its tight co...

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“…Unlabeled amino acids were added in concentrations of 1 mm (leucine, phenylalanine, and tyrosine) or 4 mm (valine). Proteoliposomes were prepared as described in reference [27] . All NMR spectroscopic experiments were conducted using 4-mm triple-resonance ( 1 H, 13 C, 15 N) probeheads at static magnetic fields of 18.8 and 14.1 T, corresponding to 1 H resonance frequencies of 800 and 600 MHz (Bruker Biospin, Karlsruhe).…”

Section: Methodsmentioning

confidence: 99%