Rainer Nikolay
@RainerNikolay
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The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding in Nat. Comms. Read here: https://t.co/Lm4ibHiuon
Joined July 2022
Excited to share our new work on the proline-rich antimicrobial peptide Api137, which disrupts large ribosomal subunit assembly and induces RNA misfolding. Big thanks to the Spahn & Hoffmann groups for this amazing collaboration! https://t.co/c9QQif03x4
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Excited to share our recent work “A Roadmap for Ribosome Assembly in Human Mitochondria” @NatureSMB A great team effort together with the groups of Henning Urlaub and @JLiepe. Fantastic work by @lavdovskaia. Thanks to everyone involved. https://t.co/VDl5pzRrX8
nature.com
Nature Structural & Molecular Biology - Lavdovskaia, Hanitsch, Linden et al. provide a comprehensive roadmap of mitoribosome biogenesis and establish that mitochondria use a unique pathway for...
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Scientists from @Beck_Laboratory, @MPIbp, @EMBL, including @iskhusainov use #cryoET #teamtomo to compare the response of human gut and laboratory E. coli strains to the antibiotic tetracycline https://t.co/MM74jkHCtQ
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Read our latest #research on antimicrobial peptides that inhibit the activity of the bacterial ribosome in multiple ways, published in @NatureComms Thx to all co-authors & the members of the Grubmüller, Hoffmann and Spahn groups. https://t.co/7mKxsw91h1
https://t.co/dVrZMP6Ej5
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Bacterial growth rate modulation is typically associated with genetic or environmental changes. In this preprint, we show that growth rate in Caulobacter varies between daughter cells in the same environment. Led by (brand-new) Dr. @skye_glenn. #ppGpp
biorxiv.org
In proliferating bacteria, growth rate is often assumed to be similar between daughter cells. However, most of our knowledge of cell growth derives from studies on symmetrically dividing bacteria. In...
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Bacterial nucleoid is a riddle wrapped in a mystery inside an enigma @JBacteriology Mini Review by Andrei Kuzminov https://t.co/BdvFe6d0kA
journals.asm.org
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I am very glad to share our paper on 30S turnover!Thank you Helge and Daniel (@WilsonLab2 ) for letting me be part of that fantastic story! I would also use the occasion to thank the collaborators and reviewers for helping us shape this work! https://t.co/lha8gKJTxJ
nature.com
Nature - Cryo-electron microscopy structures of intermediates formed during the degradation of the 30S ribosomal unit shed light on how the 3′ to 5′ exonuclease ribonuclease R controls...
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"Integrating cellular electron microscopy with multimodal data to explore biology across space and time"🔬👩💻🌌⏳ https://t.co/p6fkhe1eiH Our new review is online @CellCellPress. Big thanks to our amazing co-authors @computingCaitie @svenklumpe @RommieAmaro @KukulskiWanda @EM_STP
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Magnetic Isolation and Concentration (MagIC)-cryo-EM is a new method to enable direct structural analysis of targets captured on nanomagnetic beads, which requires only 0.0005 mg/mL of targets in 100 µL crude solution to make 10 cryo-EM grids. I will explain the magic behind it!
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Here is the original article on the “molecular de-extinction” of the antimicrobial peptides
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Check out our new study in @sciencemagazine. We show that NAC controls N-terminal methionine excision by MetAP1 in eukaryotes. Our results suggest a broader mechanism for how access of protein biogenesis factors to the translating ribosome is controlled. https://t.co/PoLECOORJv
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check out our Spotlight Article @TrendsGenetics 🔥 hot 🔥 off the press! teamed up with @OlivierDuss (@EMBLHeidelberg) & @RainerNikolay (@MPI_MolGen) to cover the recent mRNA decoding ribosome smFRET🤝cryoEM story from @TheBlanchardLab open access 👇 https://t.co/fxq2IjTQdk
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Still not where we've been @PhysikFUBerlin but on a good way to get our Krios running after the relocation to #suprafab @FU_Berlin Thanks for your patience to our users, keep fingers 🤞
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Miniature RNAs are embedded in an exceptionally protein-rich mitoribosome via an elaborate assembly pathway | Matus Valach et al. https://t.co/2cXI18kK84
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This is a really cool tool! A generator almost as amazing as nature itself.
ARE YOU SICK OF AI?! BECAUSE WE DID IT AGAIN IN AN EVEN MORE OBSCURE SPACE THAN TEXT OR IMAGES. BUCKLE UP BECAUSE THIS WONT MAKE ANY SENSE UNLESS YOU LIKE PROTEINS 💃💃🧬🧵
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Dropping the anchor, how to TRAP a ribosome at the ER membrane! Check out our new study describing a structure of TRAP complex interacting with the ribosome and Sec translocon published today in @NatureSMB
https://t.co/L7xw4Q3527
nature.com
Nature Structural & Molecular Biology - Here, the authors reveal the architecture of the TRAP complex bound to the translating ribosome and Sec61 translocon, explaining its function in...
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It's time for #MicrobeoftheMonth! Who am I? 1) I’m a zoonotic pathogen. 2) I am nonmotile. 3) I have caused 3 DNA-verified pandemics during recorded history. Think you know? Leave a guess below!
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Full Profiling of GE81112A, an Underexplored Tetrapeptide Antibiotic with Activity against Gram-Negative Pathogens - PubMed
pubmed.ncbi.nlm.nih.gov
After the first total synthesis combined with structure revision, we performed thorough in vitro and in vivo profiling of the underexplored tetrapeptide GE81112A. From the determination of the...
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Wonderful collaboration with @FilipovskaLab reveals secrets of non-canonical translation termination in mitochondria. Structural insights and ribosome profiling explain how mtRF1 recognizes noncanonical stop codons in human mitochondria. @ScienceMagazine
https://t.co/3nR16oaE1K
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Confused about biomolecular condensates? Check out our latest review: https://t.co/eMCRumNJAy Many thanks to G&D and the anonymous reviewers for an awesome review process!
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