ArticleRNA (New York, N.Y.)2008
The highest affinity binding site of small protein B on transfer messenger RNA is outside the tRNA domain.
Article in RNA (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Applications of Surface Plasmon Resonance for Advanced Studies Involving Nucleic Acids.RNA nanomed · 2024Article
- In vivo tmRNA protection by SmpB and pre-ribosome binding conformation in solution.RNA (New York, N.Y.) · 2014Article
- Active and accurate trans-translation requires distinct determinants in the C-terminal tail of SmpB protein and the mRNA-like domain of transfer messenger RNA (tmRNA).The Journal of biological chemistry · 2013Article
- The tmRNA ribosome-rescue system.Advances in protein chemistry and structural biology · 2012Review
- tmRNA-SmpB: a journey to the centre of the bacterial ribosome.The EMBO journal · 2010Article
- Visualizing the transfer-messenger RNA as the ribosome resumes translation.The EMBO journal · 2010Article
- Accommodation of tmRNA-SmpB into stalled ribosomes: a cryo-EM study.RNA (New York, N.Y.) · 2010Article
- Binding of LARP6 to the conserved 5' stem-loop regulates translation of mRNAs encoding type I collagen.Journal of molecular biology · 2010Article
- Structural features of the tmRNA-ribosome interaction.RNA (New York, N.Y.) · 2009Article
- SmpB contributes to reading frame selection in the translation of transfer-messenger RNA.Journal of molecular biology · 2009Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eubacterial ribosomes stalled on defective mRNAs are released through a mechanism referred to as trans-translation, depending on the coordinated actions of small protein B (SmpB) and transfer messenger RNA (tmRNA). A series of tmRNA variants with deletions in each structural domain were produced. Their structures were monitored by enzymatic and chemical probes in vitro, in the presence and absence of SmpB. Dissociation constants between these RNAs and SmpB from Aquifex aeolicus were derived by surface plasmon resonance (SPR) combined with filter binding assays. Three independent experimental evidences, including filter binding assays, SPR, and concentration titrations of the RNA-protein reactivity changes toward structural probes, indicate that the binding site that has the highest affinity for the protein is located outside the tRNA domain, upstream of the internal tag. The minimal tmRNA fragment that contains this high affinity site for SmpB, and also contains another site of lower affinity, includes the tag reading frame and three downstream pseudoknots that form a ring structure in solution.
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Registered trials
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.