ArticleBiophysical journal2007
Laser-induced transient grating analysis of dynamics of interaction between sensory rhodopsin II D75N and the HtrII transducer.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- Molecular model of a sensor of two-component signaling system.Scientific reports · 2021Article
- Tuning the primary reaction of channelrhodopsin-2 by imidazole, pH, and site-specific mutations.Biophysical journal · 2012Article
- Transient dissociation of the transducer protein from anabaena sensory rhodopsin concomitant with formation of the M state produced upon photoactivation.Journal of the American Chemical Society · 2011Article
- Opposite displacement of helix F in attractant and repellent signaling by sensory rhodopsin-Htr complexes.The Journal of biological chemistry · 2011Article
- The signal transfer from the receptor NpSRII to the transducer NpHtrII is not hampered by the D75N mutation.Biophysical journal · 2011Article
- Light-induced conformational change and product release in DNA repair by (6-4) photolyase.Journal of the American Chemical Society · 2011Article
- Reaction dynamics of halorhodopsin studied by time-resolved diffusion.Biophysical journal · 2009Article
- Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The interaction between sensory rhodopsin II (SRII) and its transducer HtrII was studied by the time-resolved laser-induced transient grating method using the D75N mutant of SRII, which exhibits minimal visible light absorption changes during its photocycle, but mediates normal phototaxis responses. Flash-induced transient absorption spectra of transducer-free D75N and D75N joined to 120 amino-acid residues of the N-terminal part of the SRII transducer protein HtrII (DeltaHtrII) showed only one spectrally distinct K-like intermediate in their photocycles, but the transient grating method resolved four intermediates (K(1)-K(4)) distinct in their volumes. D75N bound to HtrII exhibited one additional slower kinetic species, which persists after complete recovery of the initial state as assessed by absorption changes in the UV-visible region. The kinetics indicate a conformationally changed form of the transducer portion (designated Tr*), which persists after the photoreceptor returns to the unphotolyzed state. The largest conformational change in the DeltaHtrII portion was found to cause a DeltaHtrII-dependent increase in volume rising in 8 micros in the K(4) state and a drastic decrease in the diffusion coefficient (D) of K(4) relatively to those of the unphotolyzed state and Tr*. The magnitude of the decrease in D indicates a large structural change, presumably in the solvent-exposed HAMP domain of DeltaHtrII, where rearrangement of interacting molecules in the solvent would substantially change friction between the protein and the solvent.
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