How hibernation factors RMF, HPF, and YfiA turn off protein synthesis.

Publication Type:

Journal Article


Science, Volume 336, Issue 6083, p.915-8 (2012)


Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Escherichia coli Proteins, Models, Molecular, Peptide Chain Initiation, Translational, Prokaryotic Initiation Factors, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Ribosomal Proteins, Ribosome Subunits, Small, Bacterial, Ribosomes, RNA, Bacterial, RNA, Messenger, RNA, Ribosomal, 16S, RNA, Transfer, Thermus thermophilus


<p>Eubacteria inactivate their ribosomes as 100S dimers or 70S monomers upon entry into stationary phase. In Escherichia coli, 100S dimer formation is mediated by ribosome modulation factor (RMF) and hibernation promoting factor (HPF), or alternatively, the YfiA protein inactivates ribosomes as 70S monomers. Here, we present high-resolution crystal structures of the Thermus thermophilus 70S ribosome in complex with each of these stationary-phase factors. The binding site of RMF overlaps with that of the messenger RNA (mRNA) Shine-Dalgarno sequence, which prevents the interaction between the mRNA and the 16S ribosomal RNA. The nearly identical binding sites of HPF and YfiA overlap with those of the mRNA, transfer RNA, and initiation factors, which prevents translation initiation. The binding of RMF and HPF, but not YfiA, to the ribosome induces a conformational change of the 30S head domain that promotes 100S dimer formation.</p>