Sharing this figure from the Koonin lab: www.nature.com/articles/s41...
Worth printing large and framing

Thank you Olivier !
In a stressed P. abyssi culture, almost 50%.
It does not translocate, the C-ter remains locked in the decoding center in all 3 conformations. It's unclear how Hib, or other hibernation factors are released..

5/🧵
This work is the result of a great collaboration between labs at
@ipparis.bsky.social , @ifremer.bsky.social , @cbitoulouse.bsky.social and @pasteur.fr
Many thanks to all colleagues involved 🙌

4/🧵 - In one of these conformations, Hib blocks the peptidyl transferase center (PTC) of the large subunit by occupying both the A and P sites : A long Hib loop encircles nucleotide A2834, which separates the P and A sites, effectively locking the ribosome in an inactive state

3/🧵- High-resolution cryo-EM structures of reconstituted and in cell-extracted Hib:ribosome complexes from Pyrococcus abyssi identify three conformations encompassing the positions of tRNAs at A, P and E sites during translation.

2/🧵 - Hib adds to the growing list of archaeal ribosome hibernation factors, alongside recently identified Dri and aRDF. It is detected in all major archaeal lineages, representing about 47% of all genomes.

Our work on ribosome hibernation in archaea is out!
We identified Hib, a new hibernation factor broadly distributed across archaea.
Check out the preprint 👉 biorxiv.org/content/10.1101/2025.10.11.676729v1
(1/🧵)

yep ! and with little biomass

First ribosome purification using poly-lysine beads (RAPPL, developed by @djuranoviclab.bsky.social & collaborators: www.biorxiv.org/content/10.1...). Full process—from lysis to grid prep—in just 3 hours. Look how pretty it is (even if a bit too diluted)! This is a game-changer🚀.

A new year, a new social network and a new article in @naturecomms.bsky.social ! It unveils how archaeal RPA orchestrates the recruitment of key players in 🧬 replication primase and polD through its WH domain, with structures of both complexes!!
rdcu.be/d6GAY

We are pleased to share our work on the evolution of translation initiation now published in Nature Communications. Take a look at leaderless mRNAs and eS26 in the small ribosomal subunit of Saccharolobus solfataricus. rdcu.be/d5pgg