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Posts by Constantin Anoyatis

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A toxin/antitoxin system targeting the replication sliding-clamp induces competence in Streptococcus pneumoniae Author summary The environment in which bacteria live puts them under a great deal of stress, forcing them to adapt constantly, either temporarily or permanently. Streptococcus pneumoniae, a pathogeni...

Delighted to share a new paper from our lab, a study led by Mathieu Bergé looking at how an endogenous toxin targets replication to induce competence in the pneumococcus. dx.plos.org/10.1371/jour...

3 months ago 15 10 1 1
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Beyond RNA modification: a novel role for tRNA modifying enzyme in oxidative stress response and metabolism Abstract. RNA modifications play a fundamental role in regulating essential cellular processes, including translation fidelity and stress adaptation. While

Our new paper on DusB’s role in redox metabolism in V. cholerae is now out in @narjournal.bsky.social linking tRNAmodif enzymes and metabolic adaptation.

Beyond RNA modification: a tRNA-modifying enzyme shaping oxidative stress resilience and metabolism in V. cholerae #rnasky #rnabiology

😊🦠💫

4 months ago 41 17 8 2

What is better than one? Two connected papers!

#NewResearch

S protein of Streptococcus pneumoniae activates PBP1a and coordinates with a wider GpsB-associated multi-protein complex to regulate peptidoglycan remodelling and cell division.

#MicroSky 🦠

www.nature.com/articles/s41...

4 months ago 25 15 0 1
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AlphaSync is an enhanced AlphaFold structure database synchronized with UniProt Nature Structural & Molecular Biology, Published online: 11 November 2025; doi:10.1038/s41594-025-01719-xAlphaSync synchronizes AlphaFold Protein Structure Database predictions with UniProt sequences, providing up-to-date protein structures with residue-level annotations for humans, model organisms and pathogens through an accessible web interface and application programming interface.

New online: AlphaSync is an enhanced AlphaFold structure database synchronized with UniProt

5 months ago 6 4 0 1
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The stringent response does not influence ribosome pausing in Bacillus subtilis Abstract. The stringent response represses translation and is activated when cells enter the stationary phase and intracellular amino acid levels drop. Bac

The stringent response does not influence ribosome pausing in Bacillus subtilis

@narjournal.bsky.social from Leendert Hamoen

academic.oup.com/nar/article/...

5 months ago 5 2 0 0
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🦠🔬🤖🧑‍💻 #mAIcrobe is out! With @pinholab.bsky.social's lab, we launched an open-source framework for high-throughput bacterial image analysis. By rockstars A. Brito & B. Saraiva et al, making #DeepLearning for phenotyping accessible! Easy to use, plus model training

📜 www.biorxiv.org/content/10.1...

6 months ago 62 30 5 1
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A global view of morphogenetic peptidoglycan synthases across the domain Bacteria Abstract. Bacteria define their heritable cell shape using membrane integral glycosyltransferases (GTases) of the shape, elongation, division and sporulati

A global view of morphogenetic peptidoglycan synthases across the domain Bacteria Open Access

@femsjournals.bsky.social microLife by Francisco García-del Portillo et al

academic.oup.com/microlife/ad...

6 months ago 19 10 0 0
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Dissecting pOXA-48 fitness effects in clinical Enterobacterales using plasmid-wide CRISPRi screens Nature Communications - This study investigates the effects of the carbapenem resistance plasmid pOXA-48 in clinical enterobacteria. Using CRISPRi screens, the authors revealed that the...

This work is finally published! 🥳🧬
Plasmids are associated with very variable fitness costs in their different bacterial hosts. But, what is the contribution of each of the plasmid-genes in these host-specific effects? Study led by
@jorgesastred.bsky.social, @sanmillan.bsky.social and myself! 1/14

8 months ago 83 41 6 5
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Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota - Nature Microbiology Structural and functional characterization of the β-barrel assembly machinery complex in Bacteroidota reveals a distinct, seven-component complex with a large extracellular domain that may enable β-barrel–surface lipoprotein complex assembly.

Our paper on the Bacteroidota BAM complex is out in @natmicrobiol.nature.com! With @madejmar.bsky.social

We found that BAM in Bacteroides and Porphyromonas gingivalis has a distinct architecture from BAM in Proteobacteria.

doi.org/10.1038/s415...

6 months ago 54 23 4 2
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Role of endopeptidases in lateral cell wall expansion in Escherichia coli Peptidoglycan, the major constituent of bacterial cell walls, is a giant macromolecule made of glycan strands cross-linked by short peptides, which pr…

Proud of our new study out in @cp-cellreports.bsky.social!
Using E. coli lacking all 8 endopeptidases, we provide direct evidence that peptidoglycan expansion during elongation requires ED-mediated insertion of one glycan strand at a time. This can be performed by MepS, MepM, MepH and PBP7 #microsky

6 months ago 8 8 1 1
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(p)ppGpp-dependent activation of gene expression during nutrient limitation | mBio Bacteria often experience nutrient limitation and, in response, attenuate energetically costly metabolic processes like protein synthesis. At the same time, however, they stimulate the expression of a subset of proteins that facilitate survival under ...

(p)ppGpp-dependent activation of gene expression during nutrient limitation

#mBio from Jonathan Dworkin

journals.asm.org/doi/10.1128/...

8 months ago 6 6 0 0

Congrats @herailquentin.bsky.social

8 months ago 4 0 0 0
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Mechanism of lateral cell-wall expansion at a constant diameter in Bacillus subtilis Nature Communications - In Escherichia coli, lateral cell-wall expansion during growth occurs by crosslinking of new glycan chains to the existing peptidoglycan network. Here, Liang et al. show a...

Excited to present our new study on the mechanism of lateral peptidoglycan expansion in B. subtilis. We combined microscopy visualisation with clickable D-Ala-D-Ala analogues and stable-isotope peptidoglycan labelling to describe an inside-to-outside expansion model @natcomms.nature.com.

8 months ago 5 3 1 0
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(p)ppGpp modifies RNAP function to confer β-lactam resistance in a peptidoglycan-independent manner - Nature Microbiology The bacterial alarmone (p)ppGpp induces β-lactam resistance through modification of RNA polymerase and ribosome function rather than regulation of peptidoglycan metabolism in Escherichia coli.

Very excited to share our work on (p)ppGpp-mediated resistance to beta-lactam antibiotics published in Nature Microbiology!! A great outcome for a project we started working on 5 years ago. A big thank you to all authors that participated in this study!

www.nature.com/articles/s41...

1 year ago 2 2 0 0