A5040363648- RNA and protein synthesis mechanisms
- RNA modifications and cancer
- RNA Research and Splicing
- Enzyme Structure and Function
- Advanced Electron Microscopy Techniques and Applications
- Spectroscopy and Laser Applications
- Bacterial Genetics and Biotechnology
- Genomics and Phylogenetic Studies
- Phosphodiesterase function and regulation
- Photonic and Optical Devices
- Bacteriophages and microbial interactions
- Cold Atom Physics and Bose-Einstein Condensates
- Hepatitis C virus research
- DNA and Nucleic Acid Chemistry
- Cellular transport and secretion
- Viral Infections and Immunology Research
- Nonlinear Optical Materials Studies
- Molecular Biology Techniques and Applications
- Electron and X-Ray Spectroscopy Techniques
- Erythrocyte Function and Pathophysiology
- Animal Virus Infections Studies
- Spectroscopy Techniques in Biomedical and Chemical Research
- Cholangiocarcinoma and Gallbladder Cancer Studies
- Cholinesterase and Neurodegenerative Diseases
- Nuclear Structure and Function
Humboldt-Universität zu Berlin
2018-2024
Charité - Universitätsmedizin Berlin
2014-2024
Freie Universität Berlin
2018-2024
Max Planck Institute for Molecular Genetics
2009
Max-Planck-Institut für Kohlenforschung
2002-2003
Max Planck Society
2001-2003
Significance One of the most critical and complex steps protein synthesis elongation cycle is coupled translocation messenger (m)RNA A- P-site transfer (t)RNAs through ribosome, catalyzed by factor EF-G. This step involves large-scale molecular movements in including rotational body head 30S subunit. Previously, structures have been obtained for trapped intermediates containing a single tRNA. Here, we report cryo-EM structure an intermediate with both tRNAs. represents previously missing...
The elongation of eukaryotic selenoproteins relies on a poorly understood process interpreting in-frame UGA stop codons as selenocysteine (Sec). We used cryo-electron microscopy to visualize Sec recoding in mammals. A complex between the noncoding Sec-insertion sequence (SECIS), SECIS-binding protein 2 (SBP2), and 40 S ribosomal subunit enables Sec-specific factor eEFSec deliver Sec. SBP2 do not interact directly but rather deploy their carboxyl-terminal domains engage with opposite ends...
Translocation moves the tRNA2⋅mRNA module directionally through ribosome during elongation phase of protein synthesis. Although translocation is known to entail large conformational changes within both and tRNA substrates, orchestrated events that ensure speed fidelity this critical aspect synthesis mechanism have not been fully elucidated. Here, we present three high-resolution structures intermediates on mammalian where, in contrast bacteria, ribosomal complexes containing translocase eEF2...
Throughout the four phases of protein biosynthesis-initiation, elongation, termination, and recycling-the ribosome is controlled regulated by at least one specified translational guanosine triphosphatase (trGTPase). Although structural basis for trGTPase interaction with has been solved last three steps translation, high-resolution structure key initiation trGTPase, factor 2 (IF2), complexed ribosome, remains elusive. We determine IF2 a nonhydrolyzable triphosphate analog initiator...
Abstract In plant cells, translation occurs in three compartments: the cytosol, plastids and mitochondria. While structures of (prokaryotic-type) ribosomes mitochondria are well characterized, high-resolution eukaryotic 80S cytosol have been lacking. Here structure translating tobacco ( Nicotiana tabacum ) was solved by cryo-electron microscopy with a global resolution 2.2 Å. The ribosome includes two tRNAs, decoded mRNA nascent peptide chain, thus providing insights into molecular...
Abstract The surveillance of mRNA translation is imperative for homeostasis. Monitoring the integrity message essential, as aberrant mRNAs leads to stalling translational machinery. During ribosomal rescue, arrested ribosomes are specifically recognized by conserved eukaryotic proteins Dom34 and Hbs1, initiate their recycling. Here we solve structure Hbs1 bound a yeast ribosome programmed with nonstop at 3.3 Å resolution using cryo-electron microscopy. shows that Domain N inserted into...
Among cyclic nucleotide phosphodiesterases (PDEs), PDE6 is unique in serving as an effector enzyme G protein-coupled signal transduction. In retinal rods and cones, membrane-bound activated to hydrolyse its substrate, cGMP, by binding of two active protein α-subunits (Gα*). To investigate the activation mechanism mammalian rod PDE6, we have collected functional structural data, analysed them reaction–diffusion simulations. Gα* titration reveals a strong asymmetry with respect affinity for...
Abstract Eps15-homology domain containing proteins (EHDs) are eukaryotic, dynamin-related ATPases involved in cellular membrane trafficking. They oligomerize on membranes into filaments that induce tubulation. While EHD crystal structures open and closed conformations were previously reported, little structural information is available for the membrane-bound oligomeric form. Consequently, mechanistic insights remodeling mechanism have remained sparse. Here, by using cryo-electron tomography...
The construction of microlasers has been facilitated by mesoporous silica fibers, which are well suited to accommodate optically functional dyes and thus can lead specially designed composite systems. Construction a microcavity around dye-doped fiber leads laser light emission. emitted shows narrow system uniformly spaced resonator modes threshold behavior typical for operation (see Figure).
A novel type of laser spectroscopy for the investigation collisional dynamics atoms in close vicinity a surface has been developed. The technique utilizes excitation vapor two crossed fields, one which is directed normally to surface, whereas other excites an evanescent wave propagating along surface. results, obtained sodium near dielectric prism are quantitatively reproduced by rigorous theoretical approach. This new, nonintrusive method allows distinguish pure optical means between...