Björn M. Burmann

ORCID: 0000-0002-3135-7964
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About
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Research Areas
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Bacterial Genetics and Biotechnology
  • RNA and protein synthesis mechanisms
  • Heat shock proteins research
  • Parkinson's Disease Mechanisms and Treatments
  • Alzheimer's disease research and treatments
  • RNA Research and Splicing
  • Toxin Mechanisms and Immunotoxins
  • DNA Repair Mechanisms
  • Lipid Membrane Structure and Behavior
  • Bacteriophages and microbial interactions
  • Redox biology and oxidative stress
  • DNA and Nucleic Acid Chemistry
  • Mitochondrial Function and Pathology
  • Cellular transport and secretion
  • RNA modifications and cancer
  • Bacterial Infections and Vaccines
  • Advanced NMR Techniques and Applications
  • Signaling Pathways in Disease
  • Endoplasmic Reticulum Stress and Disease
  • Escherichia coli research studies
  • Advanced MRI Techniques and Applications
  • Glycosylation and Glycoproteins Research
  • Neuroinflammation and Neurodegeneration Mechanisms

University of Gothenburg
2018-2025

Wallenberg Wood Science Center
2020-2021

University of Basel
2011-2020

University of Bayreuth
2008-2015

Columbia University Irving Medical Center
2008-2009

Freie Universität Berlin
2009

Transcription and Translation in Train In bacteria, translation of messenger RNA into proteins by the ribosome usually begins soon after binding site emerges from polymerase. Now there is evidence for direct coupling between transcription bacteria. Proshkin et al. (p. 504 ; see Perspective Roberts ) show that trailing controls rate preventing polymerase spontaneous backtracking, which allows precise adjustment transcriptional yield to translational needs under various growth conditions....

10.1126/science.1184953 article EN Science 2010-04-22

Abstract Abnormal accumulation of misfolded and hyperphosphorylated tau protein in brain is the defining feature several neurodegenerative diseases called tauopathies, including Alzheimer’s disease (AD). In AD, this pathological change reflected by highly specific cerebrospinal fluid (CSF) biomarkers, both phosphorylated non-phosphorylated variants. Interestingly, despite pathology being at core all CSF biomarkers remain unchanged certain e.g., progressive supranuclear palsy (PSP), Pick’s...

10.1186/s13024-024-00741-9 article EN cc-by Molecular Neurodegeneration 2024-07-19

The chaperone Trigger Factor (TF) from Escherichia coli forms a dimer at cellular concentrations. While the monomer structure of TF is well known, spatial arrangement this dimeric storage form has remained unclear. Here, we determine its by combination high-resolution NMR spectroscopy and biophysical methods. symmetric head-to-tail dimer, where ribosome binding domain in contact with substrate domain, while peptidyl-prolyl isomerase contributes only slightly to affinity. highly dynamic, two...

10.1038/s41467-017-02196-7 article EN cc-by Nature Communications 2017-12-04

Abstract Mutations in glucocerebrosidase ( GBA ) are the most prevalent genetic risk factor for Lewy body disorders (LBD)—collectively Parkinson’s disease, disease dementia and with bodies. Despite this association, it remains unclear how mutations increase susceptibility to develop LBD. We investigated relationships between LBD-specific deficits, GBA-related pathways, α-synuclein levels brain tissue from LBD controls, without mutations. show that is characterised by altered sphingolipid...

10.1007/s00401-021-02367-3 article EN cc-by Acta Neuropathologica 2021-09-13

Secretion of proteins into the membrane-cell wall space is essential for cell biosynthesis and pathogenicity in Gram-positive bacteria. Folding maturation many secreted depend on a single extracellular foldase, PrsA protein. 30-kDa protein, lipid anchored to outer leaflet membrane. The crystal structure Bacillus subtilis reveals central catalytic parvulin-type prolyl isomerase domain, which inserted larger composite NC domain formed by N- C-terminal regions. This architecture resembles,...

10.1074/jbc.m114.622910 article EN cc-by Journal of Biological Chemistry 2014-12-19

Disulfide bond formation is fundamentally important for protein structure and constitutes a key mechanism by which cells regulate the intracellular oxidation state. Peroxiredoxins (PRDXs) eliminate reactive oxygen species such as hydrogen peroxide through catalytic cycle of Cys reduction. Additionally, upon PRDXs undergo extensive conformational rearrangements that may underlie their presently structurally poorly defined functions molecular chaperones. Rearrangements include high...

10.1021/jacs.3c01200 article EN cc-by Journal of the American Chemical Society 2023-05-04

Trimeric chaperone Skp activates by an unprecedented mechanism, with folding from a disordered state coupled to trimerization.

10.1126/sciadv.abc5822 article EN cc-by Science Advances 2020-10-21

The bacterial transcription factor NusG (N-utilization substance G) is suggested to act as a key coupling between and translation [Burmann, Schweimer, Luo, Wahl, Stitt, Gottesman Rösch (2010) Science 328, 501-504] contributes phage λ-mediated antitermination in Escherichia coli that enables read-through of early termination sites. E. consists two structurally functionally distinct domains are connected through flexible linker. homologous Aquifex aeolicus NusG, with secondary structure highly...

10.1042/bj20101679 article EN Biochemical Journal 2011-03-04

Mitochondria are of bacterial ancestry and have to import most their proteins from the cytosol. This process is mediated by Tom40, an essential protein that forms protein-translocating pore in outer mitochondrial membrane. Tom40 conserved virtually all eukaryotes, but its evolutionary origin unclear because orthologues not been identified so far. Recently, it was shown parasitic protozoon Trypanosoma brucei lacks a conventional instead employs archaic translocase membrane (ATOM), shows...

10.1074/jbc.m112.392118 article EN cc-by Journal of Biological Chemistry 2012-07-10

Abstract NMR spectroscopy is used to detect site‐specific intermolecular short‐range contacts in a membrane–protein–chaperone complex. This achieved by an “orthogonal” isotope‐labeling scheme that permits the unambiguous detection of NOEs between well‐folded chaperone and unfolded substrate ensemble. The residues involved these are part chaperone–substrate contact interface. approach demonstrated for 70 kDa bacterial Skp‐tOmpA

10.1002/anie.201310963 article EN Angewandte Chemie International Edition 2014-04-02

Significance FIC-domain enzymes are found in all kingdoms of life and catalyze posttranslational modifications various target proteins to modulate their function. Because the vast majority Fic expressed an inhibited form, physiological importance has escaped attention for a long time. This article reveals autonomous mechanism inhibition relief class III proteins, which hinges on autoadenylylation inhibitory helix. process occurs cis , enzyme constitutes molecular timer that operates...

10.1073/pnas.1516930113 article EN Proceedings of the National Academy of Sciences 2016-01-19

NMR spectroscopy is one of the basic tools for molecular structure elucidation. Unfortunately, resolution spectra often limited by inter-nuclear couplings. The existing workarounds alleviate problem trading it another deficiency, such as spectral artefacts or difficult sample preparation and, thus, are rarely used. We suggest an approach using coupling deconvolution in framework compressed sensing (CS) processing that leads to a major increase resolution, sensitivity, and overall quality NUS...

10.1039/d0cc06188c article EN cc-by-nc Chemical Communications 2020-01-01

Alterations in copper ion homeostasis appear coupled to neurodegenerative disorders, but mechanisms are unknown. The cytoplasmic chaperone Atox1 was recently found inhibit amyloid formation vitro of α-synuclein, the amyloidogenic protein Parkinson's disease. As α-synuclein may have copper-dependent functions, and free ions promote formation, it is important characterize interaction with on a molecular level. Here we applied solution-state nuclear magnetic resonance spectroscopy, isotopically...

10.1021/acschemneuro.9b00476 article EN ACS Chemical Neuroscience 2019-10-10

Abstract All living organisms have to cope with the constant threat of genome damage by UV light and other toxic reagents. To maintain integrity their genomes, developed a variety DNA repair pathways. One these, Transcription Coupled DNA-Repair (TCR) pathway, is triggered stalled RNA Polymerase (RNAP) complexes at sites on actively transcribed genes. A recently elucidated bacterial TCR pathway employs UvrD helicase pulling back RNAP from damage, stimulating recruitment DNA-repair machinery....

10.1038/s42003-020-01332-2 article EN cc-by Communications Biology 2020-10-23
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