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TitleStructures and dynamics of hibernating ribosomes from mediated by intermolecular interactions of HPF.
Journal, issue, pagesEMBO J, Vol. 36, Issue 14, Page 2073-2087, Year 2017
Publish dateJul 14, 2017
AuthorsIskander Khusainov / Quentin Vicens / Rustam Ayupov / Konstantin Usachev / Alexander Myasnikov / Angelita Simonetti / Shamil Validov / Bruno Kieffer / Gulnara Yusupova / Marat Yusupov / Yaser Hashem /
PubMed AbstractIn bacteria, ribosomal hibernation shuts down translation as a response to stress, through reversible binding of stress-induced proteins to ribosomes. This process typically involves the formation of ...In bacteria, ribosomal hibernation shuts down translation as a response to stress, through reversible binding of stress-induced proteins to ribosomes. This process typically involves the formation of 100S ribosome dimers. Here, we present the structures of hibernating ribosomes from human pathogen containing a long variant of the hibernation-promoting factor (SaHPF) that we solved using cryo-electron microscopy. Our reconstructions reveal that the N-terminal domain (NTD) of SaHPF binds to the 30S subunit as observed for shorter variants of HPF in other species. The C-terminal domain (CTD) of SaHPF protrudes out of each ribosome in order to mediate dimerization. Using NMR, we characterized the interactions at the CTD-dimer interface. Secondary interactions are provided by helix 26 of the 16S ribosomal RNA We also show that ribosomes in the 100S particle adopt both rotated and unrotated conformations. Overall, our work illustrates a specific mode of ribosome dimerization by long HPF, a finding that may help improve the selectivity of antimicrobials.
External linksEMBO J / PubMed:28645916 / PubMed Central
MethodsEM (single particle) / NMR (solution)
Resolution3.7 - 11.0 Å
Structure data

3624

5nd8

EMDB-3624, PDB-5nd8:
Hibernating ribosome from Staphylococcus aureus (Unrotated state)
Method: EM (single particle) / Resolution: 3.7 Å

3625

5nd9

EMDB-3625, PDB-5nd9:
Hibernating ribosome from Staphylococcus aureus (Rotated state)
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-3638:
100S disome from Staphylococcus aureus (Tight conformation)
Method: EM (single particle) / Resolution: 11.0 Å

EMDB-3639:
100S disome from Staphylococcus aureus (Loose conformation)
Method: EM (single particle) / Resolution: 9.0 Å

PDB-5nko:
Solution structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)
Method: SOLUTION NMR

Source
  • staphylococcus aureus (strain nctc 8325) (bacteria)
  • staphylococcus aureus subsp. aureus nctc 8325 (bacteria)
KeywordsRIBOSOME / S.aureus / HPF / hibernation / 100S ribosome / RIBOSOMAL PROTEIN / Staphylococcus aureus / Pathogen / Hibernating Promoting Factor

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