Author:
Razi Aida,Davis Joseph H.,Hao Yumeng,Jahagirdar Dushyant,Thurlow Brett,Basu Kaustuv,Jain Nikhil,Gomez-Blanco Josue,Britton Robert A.,Vargas Javier,Guarné Alba,Woodson Sarah A.,Williamson James R.,Ortega Joaquin
Abstract
SUMMARYTo reveal the role of the essential protein Era in the assembly of the 30S ribosomal subunit, we analyzed assembly intermediates that accumulated in Era-depleted Escherichia coli cells using quantitative mass spectrometry, cryo-electron microscopy and in-cell footprinting. Our combined approach allowed for visualization of the small subunit as it assembled and revealed that with the exception of key helices in the platform domain, all other 16S rRNA domains were able to fold even in the absence of Era. Notably, the maturing particles did not stall while waiting for the platform domain to mature and instead re-routed their folding pathway to enable concerted maturation of other structural motifs spanning multiple rRNA domains. We also found that binding of Era to the mature 30S subunit destabilized helix 44 and the decoding center preventing binding of YjeQ, another assembly factor. This work establishes Era’s role in ribosome assembly and suggests new roles in maintaining ribosome homeostasis.
Publisher
Cold Spring Harbor Laboratory
Cited by
1 articles.
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1. Why Nature Chose Potassium;Journal of Molecular Evolution;2019-10-28