One syllable > three

3. A curiosity/note of caution: just because a chaperone is found at the translating ribosome, that doesn't mean it binds the nascent polypeptide. TRiC returns to the ribosome late in p53 synthesis by hitchhiking on a mature p53 monomer that assembles with the nascent chain.

2. TRiC binding is particularly selective, for two reasons. i. It prefers specific motifs in the NC, which are only sometimes exposed. ii. Once partially folded, the nascent chain "hides" from TRiC by binding the ribosome instead. A good way to keep fragile folding intermediates safe.

A few details for the afficionados:
1. Quantitative MS of nascent chain interactomes showed how chaperones (and other proteins) are allocated to NCs. Hsp70, Hsp90 and TRiC predominate for p53, and they compete rather than follow a hierarchy.

Laura Karpauskaite in my group tackled these questions for p53, the chaperone-addicted tumour-suppressor/transcription factor.
She found that different chaperones constantly compete to bind nascent p53. Small changes in fold can tip the balance, and the ribosome ultimately decides who wins.

New from our lab @crick.ac.uk.
Nascent proteins emerge from the human ribosome into a cytosol packed with hundreds of different molecular chaperones.
Which chaperones recognise specific nascent chains, and what dictates their binding preferences?
www.biorxiv.org/content/10.6...

UK Proteostasis Meeting 2026- Submit your abstract soon!

Don’t miss the chance to present: most talks will be chosen from submitted abstracts, with poster presenters also invited to give a flash talk. ECRs are especially encouraged to apply.
Deadline: 1 May 2026
Register: forms.gle/dWz2qztKgftB...

Postdoc opening with us at EPFL!

Experimental project on how ATP driven chaperone cycles keep proteins out of equilibrium. We will quantify energy use, kinetics, and functional outcomes, including clients whose native-like functional state is stable only by sustained chaperone action.

UK Proteostasis Meeting 2026 – Reminder: Register Today


📅 20–21 July 2026 at The Francis Crick Institute, London

🗓 Abstract deadline: 1 May 2026


💷 Fees: £45 (Student/Postdoc) | £75 (Group Leader)

🔗 Register: forms.gle/dWz2qztKgftB...

🔗 Payment: www.eventbrite.co.uk/e/uk-proteos...

Proteostasis UK Logo Competition

Design our new logo and win registration, UK‑based travel, and accommodation to attend the UK Proteostasis Meeting 2026, 20–21 July at The Francis Crick Institute, London.

See here for more information:
proteostasisuk.co.uk/calls/proteo...
Deadline: 1st May 2026

Congratulations Elif!

Our recent investigation of the constriction in the bacterial ribosomal tunnel is online. Unbiased all-atom MD simulations of the entire ribosome and PDB analysis show, how flexible the constriction is. The flexibility is modulated by short nascent polypetides.

Ubiquitin & Friends Fiesta in Vienna, 29-30 April 2026.
Great speakers, small size, a friendly community, perfect for early-career researchers to connect with fellow ubiquitin enthusiasts. Sign up at www.protein-degradation.org/symposium/ and submit abstracts for talks and awards.
#ubfriends26

Please spread the word: the Structural Studies Division @mrclmb.bsky.social is looking for a new tenure-track, independent group leader with an exciting plan in any area of Structural (Molecular & Cell) biology, in discovery biology and/or methods development. 🥳

mrc.tal.net/vx/mobile-0/...

Join us at the @crick.ac.uk for the 2026 meeting of the UK proteostasis community!
We especially encourage students and postdocs to attend and share their work. All talks (except the keynotes) will be selected from abstracts.

Huge congrats to you and @niko-dalheimer.bsky.social . Great to see this out.

I'm thrilled to share our new publication, with co-first author @ Niko Dalheimer, is now out on Nature. Check out how we use live cell single particle tracking to study real time dynamics between TRiC chaperonin system and it substrates in the crowded cellular environment.

Single-molecule dynamics of the TRiC chaperonin system in vivo - Nature Single-particle tracking experiments in intact cells reveal dynamic co- and post-translational interactions of the TRiC–PFD chaperonin complex with client proteins during in vivo protein folding.

I’m excited to share my first-author paper, with co-first author @rongqinxiaoxiao.bsky.social, now out in @nature.com. We developed a live-cell single-particle tracking platform to see how TRiC & prefoldin engage proteins during co- and post-translational folding. 1/9 www.nature.com/articles/s41...

New lab paper!! We develop a technology for real-time, single-molecule visualization of proteasomal substrate degradation in cells. We find that the site of substrate engagement by the proteasome determines decay kinetics, efficiency and co-factor requirement.

www.biorxiv.org/content/10.6...

Thanks to the reviewers, and editor @kristabledsoe.bsky.social, for a smooth and constructive process, great collaborators from the Bukau and Enchev labs, and the fantastic joint lead authors @aroesel.bsky.social and @santosh-s.bsky.social

The ribosome synchronizes folding and assembly to promote oligomeric protein biogenesis Large oligomeric proteins constitute a major fraction of proteomes, but are difficult to refold in vitro, raising the question of how cells direct their biogenesis. Roeselová and Shivakumaraswamy et a...

Our latest cotranslational folding story is now published @cp-molcell.bsky.social. Really cool (I think) new ideas about how exactly the ribosome directs folding and assembly to make sure complicated proteins mature efficiently in cells.
www.cell.com/molecular-ce...

For the equivalent human complexes, see our recent paper: www.nature.com/articles/s41...

If anyone is interested in making bacterial ribosome-nascent chain complexes and studying them using HDX-MS, we have written up a detailed protocol.
rdcu.be/eYFx4
Characterise the conformational dynamics of the ribosome, nascent polypeptide and bound chaperones, label-free and at peptide-level

Join us for the #Ubiquitin & Friends Symposium 2026, April 29-30, in Vienna!
Fantastic guest speakers👇 & many slots for talks from abstracts, flash-talks & posters. Lots of opportunities to network. Register now to save your spot!
➡️ www.protein-degradation.org/symposium/
#ubfriends2026

Evolution of the ribosomal exit tunnel through the eyes of the nascent chain The ribosomal exit tunnel is a universally conserved feature of the large subunit that directs the nascent polypeptide chain into the cellular environment and is involved in co-translational folding, ...

Just in time for 2026! 🎆 Presenting a nascent-centric view on the shape of the ribosomal exit tunnel topology, based on MD-derived occupancy maps for 55 distinct ribosomes. 🧶🧬🖥️
📄 Read the preprint: biorxiv.org/content/10.6...

#StructuralBiology #Ribosome #CryoEM #Evolution #Biophysics

Thanks Paolo!

Thanks to @chercheurjuteux.com and the other reviewers - all fair and constructive.

GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome - Nature Communications The GroEL/ES chaperonin can act during protein synthesis to promote folding. Here, Roeselová et al. show how GroEL captures, remodels and sequesters nascent proteins in its central chamber, while they...

Our story on GroEL/ES action during cotranslational folding is now published @natcomms.nature.com. Led by former-student Alzbeta Roeselova, and in collaboration with Rado Enchev's lab @crick.ac.uk.
www.nature.com/articles/s41...

Postdoc (m/f/x) Our Research Group led by Janine Kirstein, Professorin at Friedrich-Schiller-University Jena, is looking for a highly motivated and talented Postdoctoral Researcher (m/f/x) to join a research project ...

Postdoc position available in my lab in Jena (Germany.
jobs.leibniz-fli.de/jobposting/6...
If you're interested in protein biochemistry of amyloid proteins and chaperones, this job may be for you. B2 Level German is required as the candidate will be involved in teaching in German.

Crick group leaders work across disciplines, supported by core funding and mentoring to build ambitious, curiosity-driven research.

Apply now to join us ➡️ www.crick.ac.uk/careers-stud...