ArticleThe Journal of biological chemistry2016
Asymmetric Functional Conversion of Eubacterial Light-driven Ion Pumps.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Harnessing light the retinal way.Nature chemistry · 2025Article
- An affordable convertible: Engineering proton transfer pathways in microbial rhodopsins.Biophysical journal · 2024Article
- Engineering yeast with a light-driven proton pump system in the vacuolar membrane.Microbial cell factories · 2024Article
- NaMolecules (Basel, Switzerland) · 2023Review
- Protein dynamics of a light-driven NaBiophysics and physicobiology · 2023Article
- Biophysical characterization of microbial rhodopsins with DSE motif.Biophysics and physicobiology · 2023Article
- Retinal-Carotenoid Interactions in a Sodium-Ion-Pumping Rhodopsin: Implications on Oligomerization and Thermal Stability.The journal of physical chemistry. B · 2023Article
- 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
- Control of Protonated Schiff Base Excited State Decay within Visual Protein Mimics: A Unified Model for Retinal Chromophores.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Article
- Functional Mechanism of ClAdvances in experimental medicine and biology · 2021Review
- History and Perspectives of Ion-Transporting Rhodopsins.Advances in experimental medicine and biology · 2021Review
- The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants.The Journal of biological chemistry · 2020Article
- Omega Rhodopsins: A Versatile Class of Microbial Rhodopsins.Journal of microbiology and biotechnology · 2020Review
- Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering.Biophysical reviews · 2017Review
- Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications.Annual review of biochemistry · 2017Review
- A natural light-driven inward proton pump.Nature communications · 2016Article
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3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In addition to the well-known light-driven outward proton pumps, novel ion-pumping rhodopsins functioning as outward Na(+) and inward Cl(-) pumps have been recently found in eubacteria. They convert light energy into transmembrane electrochemical potential difference, similar to the prototypical archaeal H(+) pump bacteriorhodopsin (BR) and Cl(-) pump halorhodopsin (HR). The H(+), Na(+), and Cl(-) pumps possess the conserved respective DTE, NDQ, and NTQ motifs in the helix C, which likely serve as their functional determinants. To verify this hypothesis, we attempted functional interconversion between selected pumps from each category by mutagenesis. Introduction of the proton-pumping motif resulted in successful Na(+) → H(+) functional conversion. Introduction of the respective characteristic motifs with several additional mutations leads to successful Na(+) → Cl(-) and Cl(-) → H(+) functional conversions, whereas remaining conversions (H(+) → Na(+), H(+) → Cl(-), Cl(-) → Na(+)) were unsuccessful when mutagenesis of 4-6 residues was used. Phylogenetic analysis suggests that a H(+) pump is the common ancestor of all of these rhodopsins, from which Cl(-) pumps emerged followed by Na(+) pumps. We propose that successful functional conversions of these ion pumps are achieved exclusively when mutagenesis reverses the evolutionary amino acid sequence changes. Dependence of the observed functional conversions on the direction of evolution strongly suggests that the essential structural mechanism of an ancestral function is retained even after the gain of a new function during natural evolution, which can be evoked by a few mutations. By contrast, the gain of a new function needs accumulation of multiple mutations, which may not be easily reproduced by limited mutagenesis in vitro.
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