Excited to share our work uncovering SNOR, a ribosome-associated factor that promotes translation restart after dormancy published in Nature!! This was, as usual, a wonderful collaborative effort between our group and the Mattei Lab @simonemattei.bsky.social @embl.org www.nature.com/articles/s41...
Video
www.cell.com/cell/abstrac...
Ahmad Jomaa
Highly conserved mRNA 3′ UTRs act as co-translational chaperones for intrinsically
disordered regions (IDRs), preventing inter-domain misfolding and enabling biogenesis
of fully active proteins.
New online: Membrane insertion of mitochondrial-encoded proteins regulates ribosome decoding speed
Meet NovoTags, a new class of fluorescent imaging probes that combines AI-driven protein design from #HHMIInvestigator David Baker w/ ultra-bright dyes from Janelia’s Luke Lavis, enabling scientists to watch dozens of proteins inside a cell at once — something current tools can't do: bit.ly/4noBb06
New online: When membrane insertion sets the pace of mitochondrial translation
Nature research paper: Single-molecule dynamics of the TRiC chaperonin system in vivo
go.nature.com/4qZM3Cn
Join scientists working on #ProteinHomeostasis in the EMBO Workshop "Proteostasis shaping health span: From protein folding to failure" in #Ericeira, #Portugal, 9–13 November 2026.
Deadline: 1 September 2026
https://meetings.embo.org/event/26-proteostasis
#EMBOproteostasis #EMBOevents 🧪
Nature Structural & Molecular Biology
HHMI
Nature Structural & Molecular Biology
EMBO
Nature
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.
Using live cell single particle tracking, we studied real time dynamics between TRiC chaperonin system and its substrates in the crowded cellular environment. Take a pook!
David Balchin
Finally out in @Cellcellpress!
Proteins with long IDRs are prone to misfolding during protein synthesis.
This is prevented by mRNA 3′UTRs that act as mRNA-based IDR chaperones.
www.cell.com/cell/fulltex...
Highly conserved mRNA 3′ UTRs act as co-translational chaperones for intrinsically
disordered regions (IDRs), preventing inter-domain misfolding and enabling biogenesis
of fully active proteins.
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.
📣 UK Proteostasis Meeting 2026 – Registration Now Open!
I’m delighted to share that registration is now open for the UK Proteostasis Meeting 2026, hosted by The Francis Crick Institute on 20–21 July 2026
.
Please register here(lnkd.in/ervXMzWN) and through Eventbrite for payment (lnkd.in/eTxqjnQy)
ProteostasisUK
Nature Structural & Molecular Biology, Published online: 07 May 2026; doi:10.1038/s41594-026-01803-wSchöndorf and Petrychenko et al. show that mitochondrial translation speed is coupled to OXA1L-mediated inner membrane insertion, with cotranslational nascent chain folding and insertion driving structural changes and translational pausing.
Nature Structural & Molecular Biology, Published online: 07 May 2026; doi:10.1038/s41594-026-01799-3Human mitochondrial ribosomes synthesize membrane proteins while docked at the inner membrane, but how insertion feeds back onto decoding has remained unclear. A recent study reveals that nascent-chain topology and early folding within the mitoribosomal vestibule modulate elongation speed, establishing kinetic checkpoints during respiratory chain biogenesis.
Nature research paper: Single-molecule dynamics of the TRiC chaperonin system in vivo
go.nature.com/4qZM3Cn
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.
