Color Change of Proteorhodopsin by a Single Amino Acid Replacement at a Distant Cytoplasmic Loop

Yoshitsugu, Maiko; Shibata, Mikihiro; Ikeda, Daisuke; Furutani, Yuji; Kandori, Hideki

doi:10.1002/anie.200705989

Cited by 30 publications

(17 citation statements)

References 32 publications

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“…In the latter case, the environment of the retinal chromophore would be influenced by A136Y in some indirect manner. Kandori and coworkers (45) recently reported a 20-nm red-shift of proteorhodopsin, a microbial-type rhodopsin in marine bacteria, by mutation of Ala 178 to Arg at the E-F loop (Fig. 2).…”

Section: Discussionmentioning

confidence: 97%

Spectral Tuning in Sensory Rhodopsin I from Salinibacter ruber

Sudo

Yuasa

Shibata

et al. 2011

Journal of Biological Chemistry

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Organisms utilize light as energy sources and as signals. Rhodopsins, which have seven transmembrane ␣-helices with retinal covalently linked to a conserved Lys residue, are found in various organisms as distant in evolution as bacteria, archaea, and eukarya. One of the most notable properties of rhodopsin molecules is the large variation in their absorption spectrum. Sensory rhodopsin I (SRI) and sensory rhodopsin II (SRII) function as photosensors and have similar properties (retinal composition, photocycle, structure, and function) except for their max (SRI, ϳ560 nm; SRII, ϳ500 nm). An expression system utilizing Escherichia coli and the high protein stability of a newly found SRI-like protein, SrSRI, enables studies of mutant proteins. To determine the residue contributing to the spectral shift from SRI to SRII, we constructed various SRI mutants, in which individual residues were substituted with the corresponding residues of SRII. Three such mutants of SrSRI showed a large spectral blue-shift (>14 nm) without a large alteration of their retinal composition. Two of them, A136Y and A200T, are newly discovered color tuning residues. In the triple mutant, the max was 525 nm. The inverse mutation of SRII (F134H/Y139A/ T204A) generated a spectral-shifted SRII toward longer wavelengths, although the effect is smaller than in the case of SRI, which is probably due to the lack of anion binding in the SRII mutant. Thus, half of the spectral shift from SRI to SRII could be explained by only those three residues taking into account the effect of Cl ؊ binding.

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Section: Discussionmentioning

confidence: 97%

Spectral Tuning in Sensory Rhodopsin I from Salinibacter ruber

Sudo

Yuasa

Shibata

et al. 2011

Journal of Biological Chemistry

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“…E. coli expressing rhodopsins was prepared in manner previously described 52,53 . The cells were collected by centrifugation (4,800g, 3 min), washed three times and resuspended in the solvent for measurement.…”

Section: Methodsmentioning

confidence: 99%

“…KR1 and KR2 having six histidines at the C terminus were expressed in E. coli C41(DE3) strain. The protein was purified via Co-affinity column (TALON, Qiagen) chromatography in manner previously described 52,53 and solubilized in 0.1% n-dodecyl-b-D-maltoside (DDM).…”

Section: Methodsmentioning

confidence: 99%

A light-driven sodium ion pump in marine bacteria

et al. 2013

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Light-driven proton-pumping rhodopsins are widely distributed in many microorganisms. They convert sunlight energy into proton gradients that serve as energy source of the cell. Here we report a new functional class of a microbial rhodopsin, a light-driven sodium ion pump. We discover that the marine flavobacterium Krokinobacter eikastus possesses two rhodopsins, the first, KR1, being a prototypical proton pump, while the second, KR2, pumps sodium ions outward. Rhodopsin KR2 can also pump lithium ions, but converts to a proton pump when presented with potassium chloride or salts of larger cations. These data indicate that KR2 is a compatible sodium ion-proton pump, and spectroscopic analysis showed it binds sodium ions in its extracellular domain. These findings suggest that light-driven sodium pumps may be as important in situ as their proton-pumping counterparts.

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“…This kind of long-range color tuning mechanisms may explain the recent experimental study that demonstrates that a single amino acid replacement in a distant cytoplasmic loop (A178R) of the proteorhodopsin causes the 20 nm red shift of λ max . 22,23 Combined theoretical and experimental studies will help to elucidate this mechanism of the color tuning in retinal proteins further.…”

mentioning

confidence: 99%

Color Tuning in Rhodopsins: The Origin of the Spectral Shift between the Chloride-Bound and Anion-Free Forms of Halorhodopsin

2012

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Detailed knowledge of the molecular mechanisms that control the spectral properties in the rhodopsin protein family is important for understanding the functions of these photoreceptors and for the rational design of artificial photosensitive proteins. Here, we used a high-level ab initio QM/MM method to investigate the mechanism of spectral tuning in the chloride-bound and anion-free forms of Halorhodopsin from Natronobacterium pharaonis (phR) and the interprotein spectral shift between them. We demonstrate that the chloride ion tunes the spectral properties of phR via two distinct mechanisms: (i) the electrostatic interaction with the chromophore that results in the 95 nm difference between the absorption maxima of the two forms and (ii) the induction of the structural reorganization in the protein that changes the positions of charged and polar residues and reduces this difference to 29 nm. The present study expands our knowledge on the role of the reorganization of the internal H-bond network for the color tuning in general and provides a detailed investigation of the tuning mechanism in phR in particular.

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Color Change of Proteorhodopsin by a Single Amino Acid Replacement at a Distant Cytoplasmic Loop

Cited by 30 publications

References 32 publications

Spectral Tuning in Sensory Rhodopsin I from Salinibacter ruber

Spectral Tuning in Sensory Rhodopsin I from Salinibacter ruber

A light-driven sodium ion pump in marine bacteria

Color Tuning in Rhodopsins: The Origin of the Spectral Shift between the Chloride-Bound and Anion-Free Forms of Halorhodopsin

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