ArticleMolecular and cellular biology2006
An arc of unpaired "hinge bases" facilitates information exchange among functional centers of the ribosome.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- The role of ribosomal protein networks in ribosome dynamics.Nucleic acids research · 2025Article
- Evolving precision: rRNA expansion segment 7S modulates translation velocity and accuracy in eukaryal ribosomes.Nucleic acids research · 2024Article
- Plant ribosomes as a score to fathom the melody of 2'-RNA biology · 2024Review
- Sordarin bound eEF2 unlocks spontaneous forward and reverse translocation on CrPV IRES.Nucleic acids research · 2023Article
- Two "Edges" in Our Knowledge on the Functions of Ribosomal Proteins: The Revealed Contributions of Their Regions to Translation Mechanisms and the Issues of Their Extracellular Transport by Exosomes.International journal of molecular sciences · 2023Review
- Mutations in RPS19 may affect ribosome function and biogenesis in Diamond Blackfan anemia.FEBS open bio · 2022Article
- Context-specific action of macrolide antibiotics on the eukaryotic ribosome.Nature communications · 2021Article
- Proteotoxic stress promotes entrapment of ribosomes and misfolded proteins in a shared cytosolic compartment.Nucleic acids research · 2020Article
- rRNA expansion segment 27Lb modulates the factor recruitment capacity of the yeast ribosome and shapes the proteome.Nucleic acids research · 2020Article
- Ribosomal protein gene RPL9 variants can differentially impair ribosome function and cellular metabolism.Nucleic acids research · 2020Article
- Iron-dependent cleavage of ribosomal RNA during oxidative stress in the yeastThe Journal of biological chemistry · 2018Article
- RNA Structural Dynamics As Captured by Molecular Simulations: A Comprehensive Overview.Chemical reviews · 2018Review
- Endonucleolytic cleavage in the expansion segment 7 of 25S rRNA is an early marker of low-level oxidative stress in yeast.The Journal of biological chemistry · 2017Article
- Tracking fluctuation hotspots on the yeast ribosome through the elongation cycle.Nucleic acids research · 2017Article
- Major centers of motion in the large ribosomal RNAs.Nucleic acids research · 2015Article
- Ribosomes in the balance: structural equilibrium ensures translational fidelity and proper gene expression.Nucleic acids research · 2014Article
- Eukaryotic rpL10 drives ribosomal rotation.Nucleic acids research · 2014Article
- Structure and mechanical properties of the ribosomal L1 stalk three-way junction.Nucleic acids research · 2012Article
- The central core region of yeast ribosomal protein L11 is important for subunit joining and translational fidelity.Molecular genetics and genomics : MGG · 2011Article
- Mutations of highly conserved bases in the peptidyltransferase center induce compensatory rearrangements in yeast ribosomes.RNA (New York, N.Y.) · 2011Article
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2 authors.
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Abstract
Information must be shared and functions coordinated among the spatially distinct functional centers of the ribosome. To address these issues, a yeast-based genetic system enabling generation of stable strains expressing only mutant forms of rRNA was devised. The B1a bridge (helix 38) has been implicated in the subtle modulation of numerous ribosomal functions. Base-specific mutations were introduced into helix 38 at sites affecting the B1a bridge and where it contacts the aminoacyl-tRNA (aa-tRNA) D-loop. Both sets of mutants promoted increased affinities for aa-tRNA but had different effects in their responses to two A-site-specific drugs and on suppression nonsense codons. Structural analyses revealed an arc of nucleotides in 25S rRNA that link the B1a bridge, the peptidyltransferase center, the GTPase-associated center, and the sarcin/ricin loop. We propose that a series of regularly spaced "hinge bases" provide fulcrums around which rigid helices can reorient themselves depending on the occupancy status of the A-site.
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