ArticlePLoS biology2014
Structural and functional insights into the mode of action of a universally conserved Obg GTPase.
Article in PLoS biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 138 citations in OpenAlex.
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- Composition and liquid-to-solid maturation of protein aggregates contribute to bacterial dormancy development and recovery.Nature communications · 2025Article
- The role of the essential GTPase ObgE in regulating lipopolysaccharide synthesis in Escherichia coli.Nature communications · 2024Article
- Late consolidation of rRNA structure during co-transcriptional assembly inbioRxiv : the preprint server for biology · 2024Article
- Miniature RNAs are embedded in an exceptionally protein-rich mitoribosome via an elaborate assembly pathway.Nucleic acids research · 2023Article
- YbiB: a novel interactor of the GTPase ObgE.Nucleic acids research · 2023Article
- At the Crossroad of Nucleotide Dynamics and Protein Synthesis in Bacteria.Microbiology and molecular biology reviews : MMBR · 2023Review
- Cryo-EM captures early ribosome assembly in action.Nature communications · 2023Article
- Protein-Ligand Interactions in Scarcity: The Stringent Response from Bacteria to Metazoa, and the Unanswered Questions.International journal of molecular sciences · 2023Review
- Novel rRNA transcriptional activity of NhaR revealed by its growth recovery for theFrontiers in molecular biosciences · 2023Article
- The structure-function analysis of Obg-like GTPase proteins along the evolutionary tree from bacteria to humans.Genes to cells : devoted to molecular & cellular mechanisms · 2022Review
- Dynamic Metabolic Response to (p)ppGpp Accumulation inFrontiers in microbiology · 2022Article
- The Role of the Universally Conserved ATPase YchF/Ola1 in Translation Regulation during Cellular Stress.Microorganisms · 2021Review
- Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Obg proteins are a family of P-loop GTPases, conserved from bacteria to human. The Obg protein in Escherichia coli (ObgE) has been implicated in many diverse cellular functions, with proposed molecular roles in two global processes, ribosome assembly and stringent response. Here, using pre-steady state fast kinetics we demonstrate that ObgE is an anti-association factor, which prevents ribosomal subunit association and downstream steps in translation by binding to the 50S subunit. ObgE is a ribosome dependent GTPase; however, upon binding to guanosine tetraphosphate (ppGpp), the global regulator of stringent response, ObgE exhibits an enhanced interaction with the 50S subunit, resulting in increased equilibrium dissociation of the 70S ribosome into subunits. Furthermore, our cryo-electron microscopy (cryo-EM) structure of the 50S·ObgE·GMPPNP complex indicates that the evolutionarily conserved N-terminal domain (NTD) of ObgE is a tRNA structural mimic, with specific interactions with peptidyl-transferase center, displaying a marked resemblance to Class I release factors. These structural data might define ObgE as a specialized translation factor related to stress responses, and provide a framework towards future elucidation of functional interplay between ObgE and ribosome-associated (p)ppGpp regulators. Together with published data, our results suggest that ObgE might act as a checkpoint in final stages of the 50S subunit assembly under normal growth conditions. And more importantly, ObgE, as a (p)ppGpp effector, might also have a regulatory role in the production of the 50S subunit and its participation in translation under certain stressed conditions. Thus, our findings might have uncovered an under-recognized mechanism of translation control by environmental cues.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.