Dr Tom Deegan from University of Edinburgh awarded The Colworth Medal by The Biochemical Society 2027 Awards.
Congratulations to Tom Deegan who receives the Colworth Medal in 2027! Pioneering work from the Deegan Lab has redefined our understanding of eukaryotic DNA replication and provided conceptual and technical frameworks that continue to drive new discoveries across molecular biology.
How important do you feel discovery research and ‘basic’ science is for understanding disease? Well, I have a little bit of a biased view on the topic, since I'm a basic scientist myself. The lab has made more and more discoveries with very strong therapeutic implications, and often people ask me why we are not pursuing these further ourselves. Part of it is that I think about this very much as an ecosystem. People have different skills – I have colleagues who are very good at the application side of things and I have other colleagues, including people in my lab, who are very good at the basic science. There are a lot of very smart people at every stage in the ecosystem and, sometimes, we have to acknowledge that we can't all be experts in every step. A lot of basic science discoveries will end up having profound implications in the clinic – if you don't have the full imagination about how to get it there, that's okay, because you're still a very important piece of the jigsaw puzzle and other people can help. If the basic science discoveries didn't exist, then it's quite possible that the well would run dry. We cannot simply rely on the idea that the therapies currently in clinical trials are going to be enough because we already know that – for diseases, such as cancer, and with rapidly evolving viruses – there needs to be a constant influx of new ideas to stay ahead of the arms race. I'd also make a plug for the fact that, ultimately, we are all interested in human disease, but disease research in humans is not ethical or possible. This is why creating and studying model organisms in a high-throughput, low-investment context is incredibly important. We cannot just say ‘okay, we're going to stop work on anything that is not related to human research’, because – actually – it's all relevant to humans.
Do you think basic science is particularly threatened by cuts to funding? Science itself is quite uncertain. We do experiments wondering if they will even work. It's discovery, and you don't know where it's going to lead. It could lead to a billion-dollar company, something like mRNA vaccines or CRISPR-Cas9 gene editing, or it could simply be something that interests you. Sometimes it might appear esoteric from the outside, but there are very smart people dedicated to this work. We shouldn't lose sight of the fact that most of this work is paid for by taxpayers, but funding uncertainty creates a very unstable foundation. If the foundations are weak, people are going to get much more conservative about the science that they're doing and worry that ‘blue-skies research’ is not worth pursuing because it won't get funded. And that would be a mistake because all innovation in science really originates from blue-skies, basic research. The second thing that uncertainty does is send a message to our young trainees – who are our future – that this is not a career option that will provide professional and personal stability. I worry that this kind of uncertainty will mean we lose an entire generation of people, and that would be a loss we might not be able to overcome.
I was interviewed by @katiepickup.bsky.social recently for @dmmjournal.bsky.social. This has a little bit of my background, a little bit on science and mentoring, and a little bit (ok, more than a little bit) on funding in science.
Check it out at: journals.biologists.com/dmm/article/...
🆕T. brucei Kozak sequences are unusual, hard to detect, but important for translation regulation - Check out the work conceived💡, carried out🔬and written up ✍️ by Philip Stettler, with only a minor contributions from me and the Polacek group - CONGRATULATIONS🎉👏 academic.oup.com/nar/article-...
Thank you so much to everyone who made it to #BSP2026 in beautiful, sunny Glasgow!!! (We asked the weather to behave while everyone was around)! The @bspparasitology.bsky.social 2027 meeting will be in Cardiff! I hope everyone enjoyed themselves! Like Glasgow, People Make #Parasitology! 🥳🧬🧫🔬
I have officially started my new position as a Senior Research Scientist at the National Institute of Infectious Diseases (NIID) 🇯🇵. My new research group will focus on the cell/molecular biology of parasitic Excavata & amoebae (incl. Trypanosoma, Naegleria, Acanthamoeba, & more) (1/3)
Logo for the 2026 BSP Spring meeting of buildings in Glasgow and parasites flying above them
Our Spring meeting starts today in Glasgow! All the best to all those presenting @bspparasitology.bsky.social
From Figure 9 showing distinct localization to the feeding apparatus
These proteins can be used for immunoprecipitation/mass spec to identify many more components, which will be key to obtaining mechanistic understanding of the feeding apparatus in diplonemids and beyond. Any feedback welcome!
Figure 7B showing that PTP2 (tyrosine protein phosphatase) localizes at apical papilla, MTR and PML (parallel microtubule loop)
In this preprint, we report 17 components that localize to feeding apparatus or flagellar apparatus (yes I love YFP-tagging screens). The feeding apparatus in diplonemids consists of cytostome (cell mouth) and cytopharynx (gullet), continuous with reinforcing microtubules. Microtubules everywhere!!
Figure 1A from the preprint showing the feeding/flagellar apparatus of a Diplonema papillatum cell. Bloody complicated!
Before that, I did not even know the terms like cytostome or cytopharynx. One reason I got interested in these structures is because Mad2 localizes at two of the three flagellar roots and reinforcing microtubules, which are important for flagellar pocket formation
When I tweeted this last year, I didn't imagine I would be studying these microtubule-based structures so soon. bsky.app/profile/bung...
New preprint! We identified many components that localize to the structure involved in "eating" in a marine organism.
#ProtistOnSky #diplonemid
www.biorxiv.org/content/10.6...
Identification of feeding apparatus components in a heterotrophic marine flagellate www.biorxiv.org/content/10.64898/2026.03...
Do we grow wiser as we age?
I spent 15+ years chasing glam journals, wasting time and energy (and frustrating my team and co-authors).
I don’t want to wake up at 70 and realize my life went into convincing a few editors my work was trendy enough.
Enough. I’ll try to be smarter.
Clicked a wrong button, re-doing the conversion without any change...
10 min and still not complete...
Waiting for a PDF-to-PDF conversion to finish
We are excited to be recruiting into 3 Associate Professorship's in @oxfordbiochemistry.bsky.social. Come join us as a colleague and benefit from our vibrant and multidisciplinary environment. Reach out to me if you have any questions. Please repost! (tinyurl.com/48deybuu) (tinyurl.com/4pdvjaft).
Before he passed away in 2021, Tom Cavalier-Smith had drafted parts of his autobiography. It's now 'published' because Gáspár Jékely put a lot of effort in! Please enjoy and share: doi.org/10.5281/zeno...
(BTW thanks Jalview @jalview.bsky.social)
mnmG/gidA (tRNA modification/maturation)
FUM1/fumC (Krebs cycle)
I am learning a lot from this debate about the last eukaryotic common ancestor. It's thought-provoking to have competing hypotheses and perspectives argued out there in the open.
Here, the two arguments are internally consistent, yet different conclusions... so where's the wrong assumption?
Multiple sequence alignment of SDHA (Complex II subunit/assembly factor) from eukaryotes and bacteria
And to repeat, I personally do not feel it is appropriate to use bacterial-origin proteins to determine the eukaryotic root. If you look at multiple sequence alignments of proteins used in Williamson 2025, the proteins look too conserved (while archaea proteins do not show that level of similarity)
What I have been arguing is that without knowing the root position, one cannot conclude that Euglenozoa (or any group) are monophyletic. You make an assumption that the root is not within Euglenozoa when you say Euglenozoa are monophyletic.
Trypanosome histone variants H3.V and H4.V promote nucleosome plasticity in repressed chromatin pubmed.ncbi.nlm.nih.gov/41709455/
If I claimed this liquid-to-solid phase transition assay on a pure protein in vitro predicts the same transition to happen in cells, what counterarguments would you raise?
Would the same counterarguments apply to a liquid-to-liquid phase transition assay on the same pure protein in vitro?
BTW when I talked to a cell biologist this week and explained that bacterial-origin proteins were used to determine the root of the eukaryotic tree of life, the person was surprised by that approach. So it's not just me who has issues with this approach.
Hey Bungo. I don't know if you figure it out but look at this one.
From this paper: shorturl.at/Og2tn
They identify this blue light receptor only in one the posterior flagelum!
That's cool! Thanks for the information. I have not figured out anything on this