🚨 New in @natmicrobiol.nature.com! We reveal how the antibiotic target PBP1b fortifies the E.coli division site against osmotic rupture. Proud this was completed in our independent labs @dmf-unil.bsky.social, with @avettiger.bsky.social. Congratulations to all authors! 🦠❄️🔬 #teamtomo bit.ly/3SCbOg1 👇

The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture - Nature Microbiology

A specific isoform of PBP1b functions independently of the activator protein, LpoB, to drive generation of a wedge-like peptidoglycan structure that strengthens the division site in Escherichia coli.

doi.org

Out now in @science.org Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape | Science www.science.org/doi/10.1126/...

Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape

Bacteria, like eukaryotes, use conserved cytoskeletal systems for intracellular organization. The plasmid-encoded ParMRC system forms actin-like filaments that segregate low–copy number plasmids. In m...

science.org

Photosynthetic bacteria helped shape Planet Earth. Among them cyanobacteria—microbes that produced the oxygen in Earth’s atmosphere & made complex life possible. They have captivated scientists for decades by offering insights into how life evolved from single cells into multicellular organisms.

Now out in its final form! www.science.org/doi/10.1126/...

Martin Loose@nartimsoole.bsky.social · last yr.

One of the most exciting discoveries from our lab so far is now online as a preprint! Read a story on how the ParMR and Min systems started to collaborate to create the CorMR cytoskeleton, which now controls cell shape in multicellular cyanobacteria: www.biorxiv.org/content/10.1...

Excited to share Alison's @alisonkickuth.bsky.social paper from the lab out in @nature.com this week! We uncovered how a mechanical ratchet mechanism drives cytokinesis in early #zebrafish embryos. Read more in this thread 🧵 and at www.nature.com/articles/s41... 🤩 @poldresden.bsky.social @mpi-cbg.de

Time to say goodbye 👋 After finishing his paper and defending his thesis, Marko is starting a new chapter as a postdoc at @cemess.bsky.social (Uni Wien). We’ll miss having you around! Congrats and all the best!

Martin Loose@nartimsoole.bsky.social · 8mo ago

Happy to share a new preprint from the lab: Marko became interested in whether the disordered linker of FtsZ might influence how the protein organizes into the Z-ring. And this led to some surprising findings! Preprint: www.biorxiv.org/content/10.1...

Happy to share a new preprint from the lab: Marko became interested in whether the disordered linker of FtsZ might influence how the protein organizes into the Z-ring. And this led to some surprising findings! Preprint: www.biorxiv.org/content/10.1...

Charge segregation in the C-terminal linker of FtsZ enables Z-ring scaling with prokaryotic cell width

Bacterial cytokinesis is orchestrated by the Z-ring, a cytoskeletal structure formed by treadmilling filaments of the tubulin-like GTPase FtsZ. During assembly, filament curvature must match the cell ...

biorxiv.org

Our fully-funded PhD program is open for applications! Join us to conduct cutting-edge research at top facilities with guidance from world-class faculty. Through our interdisciplinary training, you can tailor your PhD experience to match your interests and curiosity. Apply now: phd.ista.ac.at

The Institute of Science and Technology Austria (ISTA) @istaresearch.bsky.social is hiring a tenure-track staff scientist in Computational Structural Biology (cryo-EM, cryo-ET, structural prediction methods, image analysis)! More info here: apply.ista.ac.at/comp_structu...

Thrilled to share our newest publication in Science Advances! We uncovered how two RabGEF complexes — Mon1-Ccz1 and Fuzzy-Inturned — adapt to regulate distinct Rab GTPases despite their structurally conserved catalytic core. www.science.org/doi/full/10....

Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned

The molecular comparison of related RabGEFs reveals adaptation mechanisms of a functional module for specific cellular tasks.

science.org

We are looking for a Master’s student to join a project on in vitro reconstitution of signaling networks in pathogen–host interactions: combine protein biochemistry, fluorescence microscopy & image analysis. Deadline: September 15. Find out more and apply here: ist.ac.at/en/job/maste...

Master Thesis Position – Loose Research Group

Our Group The Loose lab at the Institute of Science and Technology Austria (ISTA) is looking for a highly motivated Master student to join our research on the in vitro reconstitution of signaling n...

ist.ac.at

We're hiring a postdoc! Join our ActinID project to explore an uncharacterized actin-binding protein. - Background in cell and/or structural biology? - Eager to bridge both fields? Get in touch if you're curious or have questions! #cellbiology #cryoEM #cryoET #actin ista.ac.at/en/job/postd...

Postdoc Research Group Schur

The Schur lab at the Institute of Science and Technology Austria (ISTA) has an open postdoc position for a highly motivated candidate to be part of our ERC-funded project ActinID. Our Group ...

ista.ac.at

One of the most exciting discoveries from our lab so far is now online as a preprint! Read a story on how the ParMR and Min systems started to collaborate to create the CorMR cytoskeleton, which now controls cell shape in multicellular cyanobacteria: www.biorxiv.org/content/10.1...

Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal system controlling cyanobacterial cell shape

Bacteria, despite their diversity, use conserved cytoskeletal systems for their intracellular organization. In unicellular bacteria, the ParMRC DNA partitioning apparatus is well known for forming act...

biorxiv.org

Looking for a student or postdoc! Want to combine evolutionary analysis + structural modeling with in vitro biochemistry & fluorescence microscopy? Help us uncover new protein-protein interactions — from in silico to in vitro. Join us at @istaresearch.bsky.social 👉 looselab.org 🧬💡🔬🎡

Very cool findings from Paula, Andrea et al.! Excited that my student Roman could contribute! See Andrea’s thread below for more details:

Andrea Vettiger@avettiger.bsky.social · last yr.

It has been coming a long way... happy to share our latest work with you: www.biorxiv.org/content/10.1... Here, we show the importance of septal fortification by the Class A Penicillin Binding Protein, PBP1b, in E. coli and provide a molecular mechanism for this function. (1/12).

🚨👉 Please check our recent work on bacterial cell division. In situ Cryo-ET reveals the cellular function of the penicillin binding protein 1b supported by AFM, live-cell imaging, in silico AlphaFold proteome screen and TIRFM. Hope you enjoy the read! #teamtomo #cryo-ET ❄️🔬🐎 big thanks to the team!

bioRxivpreprint@biorxivpreprint.bsky.social · last yr.

The aPBP-type cell wall synthase PBP1b plays a specialized role in fortifying the Escherichia coli division site against osmotic rupture https://www.biorxiv.org/content/10.1101/2025.04.02.646830v1

who doesn't enjoy some beautiful FtsZ rings on a sunday evening? these from 𝘚𝘵𝘢𝘱𝘩𝘺𝘭𝘰𝘤𝘰𝘤𝘤𝘶𝘴 𝘢𝘶𝘳𝘦𝘶𝘴, from all angles, by the @jwveening.bsky.social, posted earlier on 𝕏, on may 6, 2021 Movie S2 from journals.plos.org/plospathogen... #MicroSky

Excited about protein biochemistry, fluorescence microscopy, and image analysis? Curious how proteins drive bacterial division or define organelle identity? Join us at ISTA! Apply to the PhD program by Jan 8th: gradschool.ist.ac.at

Input needed: What is your favourite amphipathic helix? I am looking for looots of sequences to train a ML model to find even more. Please tell me! Thanks! :)