- Photoreceptor and optogenetics research
- Neuroscience and Neuropharmacology Research
- Neural dynamics and brain function
- Neuroscience and Neural Engineering
- Molecular Communication and Nanonetworks
- Photosynthetic Processes and Mechanisms
- Mass Spectrometry Techniques and Applications
- Spectroscopy and Quantum Chemical Studies
- Protist diversity and phylogeny
- Molecular spectroscopy and chirality
- Lipid Membrane Structure and Behavior
- bioluminescence and chemiluminescence research
- Environmental Toxicology and Ecotoxicology
- Genetics, Aging, and Longevity in Model Organisms
- Electron and X-Ray Spectroscopy Techniques
- Nicotinic Acetylcholine Receptors Study
- Phytochemical and Pharmacological Studies
- Genomics and Phylogenetic Studies
- Advanced Glycation End Products research
- Tissue Engineering and Regenerative Medicine
- Insect Pest Control Strategies
- Electrochemical Analysis and Applications
- Enzyme Structure and Function
- Advanced Fluorescence Microscopy Techniques
- Medicinal Plants and Bioactive Compounds
Universitätsmedizin Göttingen
2023-2024
European Neuroscience Institute Göttingen
2023-2024
University of Göttingen
2023-2024
Moscow Institute of Physics and Technology
2015-2023
Forschungszentrum Jülich
2016-2023
Moscow Power Engineering Institute
2019-2023
Lomonosov Moscow State University
2020-2023
Nanoscale Microscopy and Molecular Physiology of the Brain Cluster of Excellence 171 — DFG Research Center 103
2023
Pirogov Russian National Research Medical University
2022
Ministry of Health of the Russian Federation
2022
Neurons expressing a novel rhodopsin can be activated by light; complete story of protein structure and function follows.
High resolution structures reveal the mechanisms of sodium, potassium, and proton pumping by a light-driven microbial rhodopsin.
Abstract The light-driven sodium-pumping rhodopsin KR2 from Krokinobacter eikastus is the only non-proton cation active transporter with demonstrated potential for optogenetics. However, existing structural data on correspond exclusively to its ground state, and show no sodium inside protein, which hampers understanding of mechanism. Here we present crystal structure O-intermediate physiologically relevant pentameric form at resolution 2.1 Å, revealing a ion near retinal Schiff base,...
Rhodopsins are the most abundant light-harvesting proteins. A new family of rhodopsins, heliorhodopsins (HeRs), has recently been discovered. Unlike in known HeRs N termini face cytoplasm. The function remains unknown. We present structures bacterial HeR-48C12 two states at resolution 1.5 Å, which highlight its remarkable difference from all rhodopsins. interior HeR’s extracellular part is completely hydrophobic, while cytoplasmic comprises a cavity (Schiff base [SBC]) surrounded by charged...
Abstract Rhodopsins are ubiquitous light-driven membrane proteins with diverse functions, including ion transport. Widely distributed, they also coded in the genomes of giant viruses infecting phytoplankton where their function is not settled. Here, we examine properties OLPVR1 (Organic Lake Phycodnavirus Rhodopsin) and two other type 1 viral channelrhodopsins (VCR1s), demonstrate that VCR1s accumulate exclusively intracellularly, and, upon illumination, induce calcium release from...
Abstract Recently, two groups of rhodopsin genes were identified in large double-stranded DNA viruses. The structure and function viral rhodopsins are unknown. We present functional characterization high-resolution an Organic Lake Phycodnavirus II (OLPVRII) group 2. It forms a pentamer, with symmetrical, bottle-like central channel the narrow vestibule cytoplasmic part covered by ring 5 arginines, whereas phenylalanines form hydrophobic barrier its exit. proton donor E42 is placed helix B....
Phytoplankton is the base of marine food chain as well oxygen and carbon cycles thus plays a global role in climate ecology. Nucleocytoplasmic Large DNA Viruses that infect phytoplankton organisms regulate dynamics encompass genes rhodopsins two distinct families. Here, we present functional structural characterization proteins viral rhodopsin group 1, OLPVR1 VirChR1. Functional analysis VirChR1 shows it highly selective, Na+/K+-conducting channel and, contrast to known cation...
Abstract Light-driven sodium pumps (NaRs) are unique ion-transporting microbial rhodopsins. The major group of NaRs is characterized by an NDQ motif and has two aspartic acid residues in the central region essential for transport. Here we identify a subgroup rhodopsins bearing additional glutamic residue close vicinity to retinal Schiff base. We thoroughly characterize member this subgroup, namely protein Er NaR from Erythrobacter sp. HL-111 show that results almost complete loss pH...
A potentially universal method for the de novo solution of crystal structures membrane proteins is described.
Abstract Rhodopsins, most of which are proton pumps generating transmembrane electrochemical gradients, span all three domains life, abundant in the biosphere, and could play a crucial role early evolution life on earth. Whereas archaeal bacterial among best structurally characterized proteins, rhodopsins from unicellular eukaryotes have not been well characterized. To fill this gap current understanding to gain insight into using structure-based approach, we performed structural functional...
Abstract Transmembrane ion transport is a key process in living cells. Active of ions carried out by various transporters including microbial rhodopsins (MRs). MRs perform diverse functions such as active and passive transport, photo-sensing, others. In particular, can pump monovalent like Na + , K Cl − I NO 3 . The only characterized MR proposed to sulfate addition halides belongs the cyanobacterium Synechocystis sp. PCC 7509 named halorhodopsin ( Sy HR). structural study HR may help...
Microbial rhodopsins are retinal membrane proteins that found a broad application in optogenetics. The oligomeric state of is important for their functionality and stability. Of particular interest the cellular native environment. Fluorescence microscopy provides powerful tools to determine directly cells. Among these methods quantitative photoactivated localization (qPALM) allowing investigation molecular organization at level single protein clusters. Here, we apply qPALM investigate first...
We studied how aging affects the ability of Drosophila melanogaster to tolerate various types stress factors. Data were obtained on resistance D. oxidative and genotoxic (separately paraquat, Fe3+, Cu2+, Zn2+ ions), proteotoxic (hyperthermia, Cd2+ osmotic (NaCl) stresses, starvation, infection with pathological Beauveria bassiana fungus at different ages. In all cases, we observed a strong negative correlation between age tolerance. The largest change in age-dependent decline survival...
Abstract The new class of microbial rhodopsins, called xenorhodopsins (XeRs), [1] extends the versatility this family by inward H + pumps. [2–4] These pumps are an alternative optogenetic tool to light‐gated ion channels (e.g. ChR1,2), because activation electrically excitable cells XeRs is independent from surrounding physiological conditions. In work we functionally and spectroscopically characterized XeR Nanosalina ( Ns XeR). photodynamic behavior was investigated on ps s time scale...
Proteorhodopsins (PRs), bacterial light-driven outward proton pumps comprise the first discovered and largest family of rhodopsins, they play a significant role in life on Earth. A big remaining mystery was that up-to-date there no described rhodopsins pumping protons at acidic pH despite fact bacteria live different environment. Here we describe conceptually new which are operating as pH. comprehensive function-structure study representative clade name "mirror proteorhodopsins", from...
Abstract Phytoplankton is the base of marine food chain, oxygen, carbon cycle playing a global role in climate and ecology. Nucleocytoplasmic Large DNA Viruses regulating dynamics phytoplankton comprise genes rhodopsins two distinct families. We present function-structure characterization homologous proteins representatives family 1 viral rhodopsins, OLPVR1 VirChR1. VirChR1 highly selective, Ca 2+ -dependent, Na + /K - conducting channel and, contrast to known cation channelrhodopsins...