@biorxiv-microbiol.bsky.social
Who knew ParB-CTPase fold can kill!!!
A protein fold best known for segregating chromosomes…can be transformed into a potent antibacterial toxin in some plant and animal pathogens.
www.biorxiv.org/content/10.6...
Job alert: come to Cork 😊
Ireland, arguably one of the best English speaking countries to be a scientist these days!
Link can be a bit finicky on a phone so screen shot of main details provided too.
my.corehr.com/pls/uccrecru...
Extended Shine-Dalgarno motifs govern translation initiation in Staphylococcus aureus www.nature.com/articles/s41... 🦠
"compact pooled CRISPRi library targeting all protein-coding genes in B. subtilis and test its growth in ~150 stress conditions"
The phenotypic landscape of the model firmicute Bacillus subtilis
bioRxiv from Carol Gross
www.biorxiv.org/content/10.6...
New paper out in Nature Comms 🎉
Congrats to first author @sekid.bsky.social & thanks team & collaborators
We show that B. bifidum & E. coli can cooperate in the breastfed infant gut through nutrient cross-feeding, helping shape early-life microbiome development 🦠👶
www.nature.com/articles/s41...
Super exciting news 🚨
I am hiring a technician to join my brand new lab at the University of Birmingham! @imibirmingham.bsky.social
Come and support my BBSRC-funded research on understanding how staphylococci survive antibiotics. Please share! 🧫🧪
www.jobs.ac.uk/job/DRH271/a...
Bacterial competition drives the evolution of antibacterial mechanisms, yet how new activities arise remains poorly understood. A major route to innovation is the reuse of pre-existing genetic systems, whereby conserved protein modules are repurposed in new biological contexts to generate new capabilities. Here, we show that the ParB-CTPase fold, a conserved nucleotide-binding module best known for its role in chromosome segregation, can be functionally repurposed as an antibacterial toxin. We identify ToxB, a ParB-like domain embedded within the polymorphic toxin region of contact-dependent inhibition systems and show that it functions as a potent antibacterial effector. Structural and biochemical analyses reveal that ToxB retains the core architecture of the ParB-CTPase fold but lacks DNA-binding capability and preferentially binds ATP. This shift in nucleotide specificity underpins a distinct mode of action, in which ATP binding and hydrolysis trigger rapid nucleoid compaction, chromosome segregation defects, oxidative stress, cell chaining, and ultimately cell lysis. ToxB also exhibits toxic activity in plant cells, suggesting that it targets conserved cellular processes. Together, these findings provide direct experimental evidence that the ParB-NTPase fold is biologically versatile and can be repurposed for biological roles fundamentally distinct from its ancestral function in DNA segregation. ### Competing Interest Statement The authors have declared no competing interest. Wellcome Trust, https://ror.org/029chgv08, 221776/Z/2/Z, 227755/Z/23/Z Biotechnology and Biological Sciences Research Council, https://ror.org/00cwqg982, BB/X01097X/1 Diamond Light Source, MX32728
Great to see Sam's work on PdhD out now in Microbiology! Very cool story showing how subtle metabolic adaptations can give Staph an edge during systemic invasion #microsky
www.microbiologyresearch.org/content/jour...
Second in a recent spree of Massey lab papers published in @microbiologysociety.org - talented PhD student Kate shows how some clinical uropathogenic Staph strains have lost their ability to grow under iron-limited conditions #microsky
www.microbiologyresearch.org/content/jour...
Defining the transcriptional adaptation of Staphylococcus aureus to a range of nutritional sulfur supplementation t.co/rv79NtPwTu
Interesting insights into the role of S aureus PSMs in macrophage infection! #microsky
Tung Le
Kohl et al. combine high-resolution Ribo-seq and cryo electron microscopy to show that the bacterium Staphylococcus aureus uses extended Shine-Dalgarno motifs to initiate translation, which can make…
Firmicutes are gram-positive bacteria with important roles in human health, disease, and industry. However, more than a quarter of genes in the model firmicute Bacillus subtilis remain completely uncharacterized, including numerous core phylum-specific genes. Here, we design a compact pooled CRISPRi library targeting all protein-coding genes in B. subtilis and test its growth in ~150 stress conditions. Using data from this screen as a hypothesis generator, we perform targeted experiments that reveal that YneF, a conserved essential firmicute protein, plays a role in the SRP co-translational protein secretion pathway. We also demonstrate that ECF-transporters play a previously unknown but broadly conserved role in cell wall homeostasis, perform an unbiased analysis of amino acid crossfeeding, and make additional discoveries about bacterial competition and about the cell wall of B. subtilis. In addition to these major contributions to our understanding of B. subtilis (and gram-positive firmicutes in general), this work provides a rich dataset that will nucleate future studies of uncharacterized genes and presents a framework for accessible full-genome functional genomic screens in other bacteria. ### Competing Interest Statement The authors have declared no competing interest. National Institutes of Health, https://ror.org/01cwqze88, R35 GM118061 The University of Queensland, https://ror.org/00rqy9422
Escherichia coli is widespread in healthy breastfed infants, yet its ecological role is unclear. Here, the authors provide insights into the mechanisms supporting its persistence and co-existence with...
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Staphylococcus aureus is a leading cause of bloodstream infections causing an estimated 300,000 deaths worldwide. Using a functional genomics approach, our group previously identified that adaptation ...
www.microbiologyresearch.org
Immunity through nutrient sequestration is one of the means by which a host can protect itself from infection. As a consequence, many micro-organisms have evolved strategies to overcome this, includin...
The opportunistic pathogen <i>Staphylococcus aureus</i> proliferates within diverse host environments and consequently is a leading cause of hospital-acquired infections. During colonization <i>S. aureus</i>...
Methicillin-resistant Staphylococcus aureus (MRSA) is a key pathogenic bacterium and poses a significant therapeutic challenge due to its developing resistance to therapeutics. Here the authors establ...
