Group leader at the Francis Crick institute and head of the Protein Biogenesis lab. Interested in protein folding, ribosomes and molecular chaperones.
David Balchin
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Join scientists working on #ProteinHomeostasis in the EMBO Workshop "Proteostasis shaping health span: From protein folding to failure" in #Ericeira, #Portugal, 9ā13 November 2026.
Deadline: 1 September 2026
https://meetings.embo.org/event/26-proteostasis
#EMBOproteostasis #EMBOevents š§Ŗ
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.
"I would like to emphasize the importance of question-driven science...young scientists might enjoy science more if they are thinking about questions rather than just collecting data" journals.biologists.com/jcs/article/...
The twisted tale of cotranslational protein complex assembly
My friend Saurav wrote this with Ayala Shiber and this is a great review.
www.sciencedirect.com/science/arti...
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...
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.
