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Structures and dynamics of hibernating ribosomes from mediated by intermolecular interactions of HPF.

EMBO J.. 2017; 
Khusainov Iskander,Vicens Quentin,Ayupov Rustam,Usachev Konstantin,Myasnikov Alexander,Simonetti Angelita,Validov Shamil,Kieffer Bruno,Yusupova Gulnara,Yusupov Marat,Hashem Y
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Custom Vector Construction ) cells (Invitrogen) were trans- formed using a modified pGS21A vector (GenScript) containing SaHPF Get A Quote

摘要

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 interacti... More

关键词

cryo‐electron microscopy,hibernation,pathogen,ribo