ArticleNature structural & molecular biology2012
A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 20 citations in OpenAlex.
- RNA-Seq Analysis Revealed the Virulence Regulatory Network Mediated by the Ferric Uptake Regulator (Fur) inMicroorganisms · 2025Article
- Phi-Value and NMR Structural Analysis of a Coupled Native-State Prolyl Isomerization and Conformational Protein Folding Process.Biomolecules · 2025Article
- Direct visualization of translational GTPase factor pool formed around the archaeal ribosomal P-stalk by high-speed AFM.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Initiation of prolyl cis-trans isomerisation in the CDR-H3 loop of an antibody in response to antigen binding.Scientific reports · 2017Article
- Ribosomal protein L7/L12 is required for GTPase translation factors EF-G, RF3, and IF2 to bind in their GTP state to 70S ribosomes.The FEBS journal · 2017Article
- Subinhibitory Concentrations of Bacteriostatic Antibiotics InduceAntimicrobial agents and chemotherapy · 2017Article
- EF4 disengages the peptidyl-tRNA CCA end and facilitates back-translocation on the 70S ribosome.Nature structural & molecular biology · 2016Article
- Functional analysis of the uL11 protein impact on translational machinery.Cell cycle (Georgetown, Tex.) · 2016Article
- Functional Importance of Mobile Ribosomal Proteins.BioMed research international · 2015Review
- EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon-anticodon duplex.Nature structural & molecular biology · 2014Article
- EF-G and EF4: translocation and back-translocation on the bacterial ribosome.Nature reviews. Microbiology · 2014Review
- Common chaperone activity in the G-domain of trGTPase protects L11-L12 interaction on the ribosome.Nucleic acids research · 2012Article
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8 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
When elongation factor G (EF-G) binds to the ribosome, it first makes contact with the C-terminal domain (CTD) of L12 before interacting with the N-terminal domain (NTD) of L11. Here we have identified a universally conserved residue, Pro22 of L11, that functions as a proline switch (PS22), as well as the corresponding center of peptidyl-prolyl cis-trans isomerase (PPIase) activity on EF-G that drives the cis-trans isomerization of PS22. Only the cis configuration of PS22 allows direct contact between the L11 NTD and the L12 CTD. Mutational analyses of both PS22 and the residues of the EF-G PPIase center reveal their function in translational GTPase (trGTPase) activity, protein synthesis and cell survival in Escherichia coli. Finally, we demonstrate that all known universal trGTPases contain an active PPIase center. Our observations suggest that the cis-trans isomerization of the L11 PS22 is a universal event required for an efficient turnover of trGTPases throughout the translation process.
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