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.

yep ! and with little biomass