A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy

Linda Franken, Gerrit Oostergetel, Tjaard Pijning, Pranav Puri, Valentina Ivanovna Arkhipova, Egbert Boekema, Berend Poolman, Albert Guskov

OnderzoeksoutputAcademicpeer review

38 Citaten (Scopus)
363 Downloads (Pure)


Bacteria downregulate their ribosomal activity through dimerization of 70S ribosomes, yielding inactive 100S complexes. In Escherichia coli, dimerization is mediated by the hibernation promotion factor (HPF) and ribosome modulation factor. Here we report the cryo-electron microscopy study on 100S ribosomes from Lactococcus lactis and a dimerization mechanism involving a single protein: HPFlong. The N-terminal domain of HPFlong binds at the same site as HPF in Escherichia coli 100S ribosomes. Contrary to ribosome modulation factor, the C-terminal domain of HPFlong binds exactly at the dimer interface. Furthermore, ribosomes from Lactococcus lactis do not undergo conformational changes in the 30S head domains upon binding of HPFlong, and the Shine–Dalgarno sequence and mRNA entrance tunnel remain accessible. Ribosome activity is blocked by HPFlong due to the inhibition of mRNA recognition by the platform binding center. Phylogenetic analysis of HPF proteins suggests that HPFlong-mediated dimerization is a widespread mechanism of ribosome hibernation in bacteria.
Originele taal-2English
Aantal pagina's11
TijdschriftNature Communications
StatusPublished - 28-sep.-2017

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