The rhodopsin-transducin complex houses two distinct rhodopsin molecules
Open accessAbstract
Upon illumination the visual receptor rhodopsin (Rho) transitions to the activated form Rho(∗), which binds the heterotrimeric G protein, transducin (Gt) causing GDP to GTP exchange and Gt dissociation. Using succinylated concanavalin A (sConA) as a probe, we visualized native Rho dimers solubilized in 1mM n-dodecyl-β-d-maltoside (DDM) and Rho monomers in 5mM DDM. By nucleotide depletion and affinity chromatography together with crosslinking and size exclusion chromatography, we trapped and purified nucleotide-free Rho(∗)·Gt and sConA-Rho(∗)·Gt complexes kept in solution by either DDM or lauryl-maltose-neopentyl-glycol (LMNG). The 3 D envelope calculated from projections of negatively stained Rho(∗)·Gt-LMNG complexes accommodated two Rho molecules, one Gt heterotrimer and a detergent belt. Visualization of triple sConA-Rho(∗)·Gt complexes unequivocally demonstrated a pentameric assembly of the Rho(∗)·Gt complex in which the photoactivated Rho(∗) dimer serves as a platform for binding the Gt heterotrimer. Importantly, individual monomers of the Rho(∗) dimer in the heteropentameric complex exhibited different capabilities for regeneration with either 11-cis or 9-cis-retinal.
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The dimeric structure of rhodopsin in the complex was confirmed using succinylated concanavalin A as a labeling probe.
“The dimeric structure of rhodopsin in the complex was confirmed using succinylated concanavalin A as a labeling probe.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [345]
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Structure and Function of G-Protein-Coupled Receptor Kinases 1 and 7
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BindingDB (2017) · UC San Diego · doi:10.7270/q2jh3k1c
- Authors
- Jastrzebska, B., Ringler, P., Palczewski, K., & Engel, A.
- Affiliations
- University of Basel (CH)
- Case Western Reserve University (US)
- Corresponding author
- Palczewski, Krzysztof
- Engel, Andreas
- Venue
- Journal of Structural Biology
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 182
- Issue
- 2
- Pages
- 164-172
- ISSN
- 1047-8477 (ISSN-L)
- PMC
- PMC3633645
- OpenAlex
- W2105192362
- Cited by
- 42
- References
- 57
- Citations by year
- 2026: 1 · 2022: 2 · 2021: 1 · 2019: 2 · 2018: 2 · 2017: 4 · 2016: 5 · 2015: 5 · 2014: 7 · 2013: 13
- FWCI
- 4.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Journal of Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- edoc (University of Basel) (submittedVersion)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (3100A0-108299)
- National Institutes of Health (EY019478, EY008061, U54GM094598)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- rhodopsin, transducin, G protein activation, pentameric complex, retinal isomerization, detergent solubilization, concanavalin A binding
- MeSH terms
- Chromatography, Affinity, Chromatography, Gel, Concanavalin A, Glucosides, Models, Molecular, Protein Conformation, Rhodopsin, Immunoblotting, Transducin, Dimerization, Macromolecular Substances
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