ArticleBiophysical journal2006
Role of the cytoplasmic domain in Anabaena sensory rhodopsin photocycling: vectoriality of Schiff base deprotonation.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- HwMR is a novel magnesium-associated protein.Biophysical journal · 2022Article
- Specific residues in the cytoplasmic domain modulate photocurrent kinetics of channelrhodopsin from Klebsormidium nitens.Communications biology · 2021Article
- Probing Channelrhodopsin Electrical Activity in Algal Cell Populations.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Unifying photocycle model for light adaptation and temporal evolution of cation conductance in channelrhodopsin-2.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Unusual Stability of Anabaena Sensory Rhodopsin Transducer fromThe international journal of engineering and science · 2017Article
- A natural light-driven inward proton pump.Nature communications · 2016Article
- Photo-induced regulation of the chromatic adaptive gene expression by Anabaena sensory rhodopsin.The Journal of biological chemistry · 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
- An inward proton transport using Anabaena sensory rhodopsin.Journal of microbiology (Seoul, Korea) · 2011Review
- His-75 in proteorhodopsin, a novel component in light-driven proton translocation by primary pumps.The Journal of biological chemistry · 2009Article
- Photoreactions and structural changes of anabaena sensory rhodopsin.Sensors (Basel, Switzerland) · 2009Article
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
Light-induced electric signals in intact E. coli cells generated by heterologously expressed full-length and C-terminally truncated versions of Anabaena sensory rhodopsin (ASR) demonstrate that the charge movements within the membrane-embedded part of the molecule are stringently controlled by the cytoplasmic domain. In particular, truncation inverts the direction of proton movement during Schiff base deprotonation from outward to cytoplasmic. Truncation also alters faster charge movements that occur before Schiff base deprotonation. Asp(217) as previously shown by FTIR serves as a proton acceptor in the truncated ASR but not in the full-length version, and its mutation to Asn restores the natural outward direction of proton movement. Introduction of a potential negative charge (Ser(86) to Asp) on the cytoplasmic side favors a cytoplasmic direction of proton release from the Schiff base. In contrast, mutation of the counterion Asp(75) to Glu reverses the photocurrent to the outward direction in the truncated pigment, and in both truncated and full-length versions accelerates Schiff base deprotonation more than 10-fold. The communication between the cytoplasmic domain and the membrane-embedded photoactive site of ASR demonstrated here is likely to derive from the receptor's use of a cytoplasmic protein for signal transduction, as has been suggested previously from binding studies.
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