A5005343417- Photoreceptor and optogenetics research
- Retinal Development and Disorders
- Receptor Mechanisms and Signaling
- CRISPR and Genetic Engineering
- RNA and protein synthesis mechanisms
- RNA Research and Splicing
- Bacterial Genetics and Biotechnology
- Monoclonal and Polyclonal Antibodies Research
- Photosynthetic Processes and Mechanisms
- Molecular spectroscopy and chirality
- Amino Acid Enzymes and Metabolism
- Retinopathy of Prematurity Studies
- Prion Diseases and Protein Misfolding
Paul Scherrer Institute
2022-2024
ETH Zurich
2024
University of Zurich
2020
Abstract Vision is initiated by the rhodopsin family of light-sensitive G protein-coupled receptors (GPCRs) 1 . A photon absorbed 11- cis retinal chromophore rhodopsin, which isomerizes within 200 femtoseconds to all- trans conformation 2 , thereby initiating cellular signal transduction processes that ultimately lead vision. However, intramolecular mechanism photoactivated induces activation events inside remains experimentally unclear. Here we use ultrafast time-resolved crystallography at...
Abstract Bacterial and archaeal CRISPR-Cas systems provide RNA-guided immunity against genetic invaders such as bacteriophages plasmids. Upon target RNA recognition, type III produce cyclic-oligoadenylate second messengers that activate downstream effectors, including Csm6 ribonucleases, via their CARF domains. Here, we show Enteroccocus italicus (EiCsm6) degrades its cognate cyclic hexa-AMP (cA6) activator, report the crystal structure of EiCsm6 bound to a cA6 mimic. Our structural,...
Abstract Animal vision depends on opsins, a category of G protein-coupled receptor (GPCR) that achieves light sensitivity by covalent attachment to retinal. Typically binding as an inverse agonist in the 11-cis form, retinal photoisomerizes all-trans isomer and activates receptor, initiating downstream signaling cascades. Retinal bound bistable opsins isomerizes back state after absorption second photon, inactivating receptor. Bistable are essential for invertebrate non-visual perception...
Animal vision depends on opsins, a category of G protein-coupled receptor (GPCR) that achieves light sensitivity by covalent attachment to retinal. Typically binding as an inverse agonist, 11-cis retinal photoisomerizes the all-trans isomer and activates receptor, initiating downstream signaling cascades. Retinal bound bistable opsins isomerizes back state after absorption second photon, inactivating receptor. Bistable are essential for invertebrate nonvisual perception across animal...
Abstract Vision is initiated by the rhodopsin family of light-sensitive G protein-coupled receptors (GPCRs). A photon absorbed 11- cis retinal chromophore which isomerises within 200 femtoseconds to all- trans conformation, thereby initiating cellular signal transduction processes that ultimately lead vision. However, intramolecular mechanism photoactivated induces activation events inside remains elusive. In this work, we use ultrafast time-resolved crystallography at room temperature...
Abstract Opsins are G protein-coupled receptors (GPCRs) that have evolved to detect light stimuli and initiate intracellular signaling cascades. Their role as signal transducers is critical perception across the animal kingdom. covalently bind chromophore 11-cis retinal, which isomerizes all-trans isomer upon photon absorption, causing conformational changes result in receptor activation. Monostable opsins, responsible for vision vertebrates, release after activation must another retinal...
Opsins are G protein-coupled receptors (GPCRs) that have evolved to detect light stimuli and initiate intracellular signaling cascades. Their role as signal transducers is critical perception across the animal kingdom. covalently bind chromophore 11-cis retinal, which isomerizes all-trans isomer upon photon absorption, causing conformational changes result in receptor activation. Monostable opsins, responsible for vision vertebrates, release after activation must another retinal molecule...
Withdrawal Statement The authors have withdrawn their manuscript owing to several irregularities that recently come light. Therefore, the do not wish this work be cited as reference for project. If you any questions, please contact corresponding author.
Abstract Upon target RNA recognition, type III CRISPR-Cas systems produce cyclic oligoadenylate second messengers to activate downstream effectors including Csm6-family ribonucleases via their CARF domains. Here we show that Enteroccocus italicus Csm6 (EiCsm6) degrades its cognate hexa-AMP (cA6) activator and report the crystal structure of EiCsm6 bound a cA6 mimic. The structure, combined with biochemical in vivo functional assays, reveal how recognition by domain activates HEPN domains for...