ArticleJournal of molecular biology2015
Functional consequences of the oligomeric assembly of proteorhodopsin.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 47 citations in OpenAlex.
- Coarse-Grained Molecular Dynamics Simulations Reveal Potential Role of Cardiolipin in Lateral Organization of Proteorhodopsin.Biochemistry · 2025Article
- Long-Time Scale Simulations Reveal Key Dynamics That Drive the Onset of the N State in the Proteorhodopsin Photocycle.The journal of physical chemistry. B · 2024Article
- Structural insights into the mechanism and dynamics of proteorhodopsin biogenesis and retinal scavenging.Nature communications · 2024Article
- Article
- NaMolecules (Basel, Switzerland) · 2023Review
- Protein dynamics of a light-driven NaBiophysics and physicobiology · 2023Article
- Lipid membrane mimetics and oligomerization tune functional properties of proteorhodopsin.Biophysical journal · 2023Article
- Solid-State NMR Spectroscopy on Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Cryo-EM structure and dynamics of the green-light absorbing proteorhodopsin.Nature communications · 2021Article
- Spectroscopic Characterization of Halorhodopsin Reconstituted into Nanodisks Using Native Lipids.Biophysical journal · 2020Article
- Electrostatic Environment of Proteorhodopsin Affects the pKa of Its Buried Primary Proton Acceptor.Biophysical journal · 2020Article
- Cryo-electron microscopic and X-ray crystallographic analysis of the light-driven proton pump proteorhodopsin reveals a pentameric assembly.Journal of structural biology: X · 2020Article
- Proper evaluation of chemical cross-linking-based spatial restraints improves the precision of modeling homo-oligomeric protein complexes.BMC bioinformatics · 2019Article
- X-ray Crystallographic Structure and Oligomerization of Gloeobacter Rhodopsin.Scientific reports · 2019Article
- Functional importance of the oligomer formation of the cyanobacterial HScientific reports · 2019Article
- Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Strong pH-Dependent Near-Infrared Fluorescence in a Microbial Rhodopsin Reconstituted with a Red-Shifting Retinal Analogue.The journal of physical chemistry letters · 2018Article
- Functionally Active Membrane Proteins Incorporated in Mesostructured Silica Films.Journal of the American Chemical Society · 2018Article
- Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications.Annual review of biochemistry · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The plasma membrane is the crucial interface between the cell and its exterior, packed with embedded proteins experiencing simultaneous protein-protein and protein-membrane interactions. A prominent example of cell membrane complexity is the assembly of transmembrane proteins into oligomeric structures, with potential functional consequences that are not well understood. From the study of proteorhodopsin (PR), a prototypical seven-transmembrane light-driven bacterial proton pump, we find evidence that the inter-protein interaction modulated by self-association yields functional changes observable from the protein interior. We also demonstrate that the oligomer is likely a physiologically relevant form of PR, as crosslinking of recombinantly expressed PR reveals an oligomeric population within the Escherichia coli membrane (putatively hexameric). Upon chromatographic isolation of oligomeric and monomeric PR in surfactant micelles, the oligomer exhibits distinctly different optical absorption properties from monomeric PR, as reflected in a prominent decrease in the pKa of the primary proton acceptor residue (D97) and slowing of the light-driven conformational change. These functional effects are predominantly determined by specific PR-PR contacts over nonspecific surfactant interactions. Interestingly, varying the surfactant type alters the population of oligomeric states and the proximity of proteins within an oligomer, as determined by sparse electron paramagnetic resonance distance measurements. Nevertheless, the dynamic surfactant environment retains the key function-tuning property exerted by oligomeric contacts. A potentially general design principle for transmembrane protein function emerges from this work, one that hinges on specific oligomeric contacts that can be modulated by protein expression or membrane composition.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.