Jan Löwe
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Articles by Jan Löwe
Eukaryotic-like microtubules and dynamic instability of Asgard archaeal tubulins
Abstract INTRODUCTION RESULTS DISCUSSION MATERIALS AND METHODS Acknowledgments Supplementary Materials REFERENCES Information & Authors Metrics & Citations View Options References Figures Tables Media Share Abstract Eukaryotic cells change their shapes, actively segregate their DNA, and contain membrane networks, facilitated by a complex cytoskeleton containing actin filaments, microtubules made from tubulin, and other components.
Mechanism of DNA capture by the MukBEF SMC complex and its inhibition by a viral DNA mimic
Keywords SMC complexes MukBEF Wadjet condensin cohesin cryo-EM DNA mimics bacteriophages Introduction Large ring-like structural maintenance of chromosome (SMC) complexes are fundamental chromosome organizers and facilitate diverse DNA transactions in bacteria, archaea, and eukaryotes.1,2,3 They mediate mitotic and meiotic chromosome compaction, sister chromatid cohesion, folding of chromosomes, DNA recombination, double-strand break repair, silencing of viral genomes, and the restriction of...
Nowcasting Solar Energetic Particle Events for Mars Missions
1 Motivation and Introduction The deep-space radiation environment is primarily influenced by two sources due to their high energy and prolonged exposure: sporadic eruptive events consisting of Solar Energetic Particles (SEPs) and the omnipresent Galactic Cosmic Rays (GCRs). The latter originate outside the solar system, primarily from supernovae and neutron star mergers (for nuclei with Z ⋗ ${\gtrdot}$ 30) (Drout et al., 2017).
Membraneless channels sieve cations in ammonia-oxidizing marine archaea - Nature
Abstract Nitrosopumilus maritimus is an ammonia-oxidizing archaeon that is crucial to the global nitrogen cycle1,2. A critical step for nitrogen oxidation is the entrapment of ammonium ions from a dilute marine environment at the cell surface and their subsequent channelling to the cell membrane of N. maritimus.
Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division - Nature Microbiology
Abstract Cell division in all domains of life requires the orchestration of many proteins, but in Archaea most of the machinery remains poorly characterized. Here we investigate the FtsZ-based cell division mechanism in Haloferax volcanii and find proteins containing photosynthetic reaction centre (PRC) barrel domains that play an essential role in archaeal cell division. We rename these proteins cell division protein B 1 (CdpB1) and CdpB2.
What AlphaFold tells us about cohesin’s retention on and release from chromosomes
eLife assessment This important study makes use of AlphaFold2 to predict the models of tens of cohesin subcomplexes from different species. The models, which are in most cases consistent with published cohesin variants with compromised in vitro and in vivo cohesin activity, provide convincing evidence that leads to testable hypotheses of cohesin dynamics and regulation.
What Alphafold tells us about cohesin's retention and release from chromosomes
Abstract Cohesin is a trimeric complex containing a pair of SMC proteins (Smc1 and Smc3) whose ATPase domains at the end of long coiled coils (CC) are interconnected by Scc1. During interphase, it organizes chromosomal DNA topology by extruding loops in a manner dependent on Scc1's association with two large hook shaped proteins called SA (yeast: Scc3) and Nipbl (Scc2).
Filament structure and subcellular organization of the bacterial intermediate filament-like protein crescentin
New Results doi: https://doi.org/10.1101/2023.06.04.543601 Abstract The coiled coil protein crescentin is required for the crescent shape of the freshwater bacterium Caulobacter crescentus (vibrioides). Crescentin forms a filamentous structure on the inner, concave side of the curved cells.
Mysterious Asgard archaea microbes reveal their inner secrets
Spang, A. et al. Nature 521, 173–179 (2015). Article PubMed Google Scholar Rodrigues-Oliviera, T. et al. Nature https://doi.org/10.1038/s41586-022-05550-y (2022). Article Google Scholar Imachi, H. et al. Nature 577, 519–525 (2020). Article PubMed Google Scholar Baum, D. A. & Baum, B. BMC Biol. 12, 76 (2014). Article PubMed Google Scholar Spang, A. et al. PLoS Genet. 14, e1007080 (2018). Article PubMed Google Scholar Schwartz, R. M. & Dayhoff, M. O. Science 199, 395–403 (1978).
Asgard archaea shed light on the evolutionary origins of the eukaryotic ubiquitin-ESCRT machinery - Nature Communications
Abstract The ESCRT machinery, comprising of multiple proteins and subcomplexes, is crucial for membrane remodelling in eukaryotic cells, in processes that include ubiquitin-mediated multivesicular body formation, membrane repair, cytokinetic abscission, and virus exit from host cells.
Cryo‐EM structure of the full‐length Lon protease from Thermus thermophilus
Abstract In bacteria, Lon is a large hexameric ATP-dependent protease that targets misfolded and also folded substrates, some of which are involved in cell division and survival of cellular stress. The N-terminal domain of Lon facilitates substrate recognition, but how the domains confer such activity has remained unclear. Here, we report the full-length structure of Lon protease from Thermus thermophilus at 3.9 Å resolution in a substrate-engaged state.
Bacterial and archaeal cytoskeletons
Summary All living cells depend on the intricate organization of molecular components in space and time. Although this notion was historically based on eukaryotic cells, with their structured intracellular architecture and cellular morphologies, it is now recognized that prokaryotes (that is, bacteria and archaea) also possess complex structures.
FtsK in motion reveals its mechanism for double-stranded DNA translocation
FtsK in motion reveals its mechanism for double-stranded DNA translocation Nicolas L. Jean, Trevor J. Rutherford, Jan Löwe Proceedings of the National Academy of Sciences Jun 2020, 202001324; DOI: 10.1073/pnas.2001324117
Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution
Abstract Positioning of the division site in many bacterial species relies on the MinCDE system, which prevents the cytokinetic Z-ring from assembling anywhere but the mid-cell, through an oscillatory diffusion-reaction mechanism. MinD dimers bind to membranes and, via their partner MinC, inhibit the polymerization of cell division protein FtsZ into the Z-ring. MinC and MinD form polymeric assemblies in solution and on cell membranes.
Prokaryotic cytoskeletons: protein filaments organizing small cells
1.Bi, E. & Lutkenhaus, J. FtsZ ring structure associated with division in Escherichia coli. Nature 354, 161–164 (1991).2.de Boer, P., Crossley, R. & Rothfield, L. The essential bacterial cell-division protein FtsZ is a GTPase. Nature 359, 254–256 (1992).3.RayChaudhuri, D. & Park, J. T. Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature 359, 251–254 (1992).4.Löwe, J. & Amos, L. A. Crystal structure of the bacterial cell-division protein FtsZ.
Structural Insights into Ring Formation of Cohesin and Related Smc Complexes
Cohesin facilitates sister chromatid cohesion through the formation of a large ring structure that encircles DNA. Its function relies on two structural maintenance of chromosomes (Smc) proteins, which are found in almost all organisms tested, from bacteria to humans. In accordance with their ubiquity, Smc complexes, such as cohesin, condensin, Smc5-6, and the dosage compensation complex, affect almost all processes of DNA homeostasis.
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