ArticleNucleic acids research2012
Common chaperone activity in the G-domain of trGTPase protects L11-L12 interaction on the ribosome.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- The GTPase BipA expressed at low temperature inThe Journal of biological chemistry · 2018Article
- 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
- EF4 disengages the peptidyl-tRNA CCA end and facilitates back-translocation on the 70S ribosome.Nature structural & molecular biology · 2016Article
- 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
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translational GTPases (trGTPases) regulate all phases of protein synthesis. An early event in the interaction of a trGTPase with the ribosome is the contact of the G-domain with the C-terminal domain (CTD) of ribosomal protein L12 (L12-CTD) and subsequently interacts with the N-terminal domain of L11 (L11-NTD). However, the structural and functional relationships between L12-CTD and L11-NTD remain unclear. Here, we performed mutagenesis, biochemical and structural studies to identify the interactions between L11-NTD and L12-CTD. Mutagenesis of conserved residues in the interaction site revealed their role in the docking of trGTPases. During docking, loop62 of L11-NTD protrudes into a cleft in L12-CTD, leading to an open conformation of this domain and exposure of hydrophobic core. This unfavorable situation for L12-CTD stability is resolved by a chaperone-like activity of the contacting G-domain. Our results suggest that all trGTPases-regardless of their different specific functions-use a common mechanism for stabilizing the L11-NTD•L12-CTD interactions.
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