Role of Era in assembly and homeostasis of the ribosomal small subunit.
Base Sequence
Binding Sites
Cryoelectron Microscopy
Escherichia coli Proteins
/ genetics
GTP Phosphohydrolases
/ genetics
GTP-Binding Proteins
/ genetics
Homeostasis
Nucleic Acid Conformation
Protein Binding
RNA, Ribosomal, 16S
/ chemistry
RNA-Binding Proteins
/ genetics
Ribosomal Proteins
/ genetics
Ribosome Subunits, Small
/ genetics
Ribosome Subunits, Small, Bacterial
/ genetics
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
05 09 2019
05 09 2019
Historique:
accepted:
27
06
2019
revised:
11
06
2019
received:
07
03
2019
pubmed:
3
7
2019
medline:
18
12
2019
entrez:
3
7
2019
Statut:
ppublish
Résumé
Assembly factors provide speed and directionality to the maturation process of the 30S subunit in bacteria. To gain a more precise understanding of how these proteins mediate 30S maturation, it is important to expand on studies of 30S assembly intermediates purified from bacterial strains lacking particular maturation factors. To 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, high resolution 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 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.
Identifiants
pubmed: 31265110
pii: 5527280
doi: 10.1093/nar/gkz571
pmc: PMC6736133
doi:
Substances chimiques
Escherichia coli Proteins
0
RNA, Ribosomal, 16S
0
RNA-Binding Proteins
0
Ribosomal Proteins
0
era protein, E coli
0
GTP Phosphohydrolases
EC 3.6.1.-
GTP-Binding Proteins
EC 3.6.1.-
RsgA protein, E coli
EC 3.6.1.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8301-8317Subventions
Organisme : NIA NIH HHS
ID : R00 AG050749
Pays : United States
Organisme : NIH HHS
ID : S10 OD021567
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM110248
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM060819
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM053757
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM136351
Pays : United States
Organisme : CIHR
ID : PJT-153044
Pays : Canada
Informations de copyright
© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.
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