A5060010220- RNA and protein synthesis mechanisms
- Bacterial Genetics and Biotechnology
- Enzyme Structure and Function
- RNA Research and Splicing
- RNA modifications and cancer
- Peptidase Inhibition and Analysis
- Cellular transport and secretion
- Photosynthetic Processes and Mechanisms
- Heat shock proteins research
- Protein Structure and Dynamics
- Biochemical and Molecular Research
- Lipid Membrane Structure and Behavior
- Ubiquitin and proteasome pathways
- Endoplasmic Reticulum Stress and Disease
- Enzyme Production and Characterization
- Listeria monocytogenes in Food Safety
- Mitochondrial Function and Pathology
- Photoreceptor and optogenetics research
- Toxin Mechanisms and Immunotoxins
- Bacteriophages and microbial interactions
- Signaling Pathways in Disease
- Mycobacterium research and diagnosis
- Various Chemistry Research Topics
- Nuclear Structure and Function
- Phytase and its Applications
Heidelberg University
2016-2025
Heidelberg University
2008-2024
European Molecular Biology Laboratory
1997-2023
Weizmann Institute of Science
2023
University of Geneva
2023
DKFZ-ZMBH Alliance
2002-2023
Turku Centre for Biotechnology
2013
University of Turku
2013
The University of Tokyo
2012
MRC Laboratory of Molecular Biology
2012
Eukaryotic 60S ribosomal subunits are comprised of three rRNAs and ∼50 proteins. The initial steps their formation take place in the nucleolus, but, owing to a lack structural information, this process is poorly understood. Using cryo-EM, we solved structures early biogenesis intermediates at 3.3 Å 4.5 resolution, thereby providing insights into sequential folding assembly pathway. Besides revealing distinct immature rRNA conformations, map 25 factors six different states. Notably,...
Intron removal during pre-mRNA splicing is of extraordinary complexity and its disruption causes a vast number genetic diseases in humans. While key steps the canonical spliceosome cycle have been revealed by combined structure–function analyses, structural information on an aberrant committed to premature disassembly not available. Here, we report two cryo-electron microscopy structures post-Bact intermediates from Schizosaccharomyces pombe primed for disassembly. We identify DEAH-box...
Signal recognition particle (SRP), together with its receptor (SR), mediates the targeting of ribosome-nascent chain complexes to endoplasmic reticulum. Using protein cross-linking, we detected distinct modes in binding SRP ribosome. During signal peptide recognition, SRP54 is positioned at exit site close ribosomal proteins L23a and L35. When contacts SR, rearranged such that it no longer L23a. This repositioning may allow translocon dock ribosome, leading insertion into translocation channel.
The GTPase Arf1 is considered as a molecular switch that regulates binding and release of coat proteins polymerize on membranes to form transport vesicles. Here, we show Arf1-GTP induces positive membrane curvature find the small can dimerize dependent GTP. Investigating possible link between Arf dimerization formation, isolated an mutant cannot dimerize. Although it was capable exerting classical role receptor, could not mediate formation COPI vesicles from Golgi-membranes lethal when...
Flagella are the bacterial organelles of motility and can play important roles in pathogenesis. biosynthesis requires coordinated export huge protein amounts from cytosol to nascent flagellar structure at cell surface employs a type III secretion system (T3SS). Here we show that integral membrane FlhA gram-positive bacterium Bacillus subtilis acts as an adaptor for late substrates T3SS. The major filament (flagellin) filament-cap (FliD) bind cytoplasmic domain (FlhA-C) only complex with...
The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, middle domain (MD) is a coiled-coil propeller that binds Hsp70. Although subunit structure known, positioning of MD hexamer and its mechanism action are unclear. We obtained electron microscopy (EM) structures BAP variant protease ClpP, clearly revealing density on surface ring. Mutant analysis asymmetric reconstructions show MDs adopt diverse positions single...
Tail-anchored (TA) proteins are involved in cellular processes including trafficking, degradation, and apoptosis. They contain a C-terminal membrane anchor posttranslationally delivered to the endoplasmic reticulum (ER) by Get3 adenosine triphosphatase interacting with hetero-oligomeric Get1/2 receptor. We have determined crystal structures of complex cytosolic domains Get1 Get2 different functional states at 3.0, 3.2, 4.6 angstrom resolution. The structural data, together biochemical...
COPI coated vesicles mediate trafficking within the Golgi apparatus and between endoplasmic reticulum. Assembly of a vesicle is initiated by small GTPase Arf1 that recruits coatomer complex to membrane, triggering polymerization budding. The uncoats before fusion with target membrane. Coat components are structurally conserved clathrin/adaptor proteins. Using cryo-electron tomography subtomogram averaging, we determined structure coat assembled on membranes in vitro at 9 Å resolution. We...
Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from ribosome. This results in their targeting to docking with SRP receptor, which facilitates transfer ribosome translocon. Here, we present 8 angstrom cryo-electron microscopy structure a "docking complex" consisting SRP-bound 80S receptor. Interaction receptor both rearranged S domain such that ribosomal binding site for translocon, L23e/L35 site, became exposed,...