ArticleBiophysical chemistry2021
smFRET study of rRNA dimerization at the peptidyl transfer center.
Article in Biophysical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- On the Re-Creation of Protoribosome Analogues in the Lab.International journal of molecular sciences · 2024Review
- Minimization of the E. coli ribosome, aided and optimized by community science.Nucleic acids research · 2024Article
- The Peptidyl Transferase Center: a Window to the Past.Microbiology and molecular biology reviews : MMBR · 2021Article
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Authors and funding
2 authors.
Funding
Abstract
The ribosome is a ribozyme. At the peptidyl transfer center (PTC) of 180 nt, two loops (the A- and P- loops) bind to tRNAs and position them in close proximity for efficient peptidyl ligation. There is also a 2-fold rotational symmetry in the PTC, which suggests that the precursor of the modern ribosome possibly emerged through dimerization and gene fusion. However, experiments that demonstrate the possible dimerization have not yet been published. In our investigation, we reported single molecule FRET studies of two RNA fragments that generated high FRET values. By dye-labeling the 5'-biotinylated rRNA molecules at the 3'- terminals, or labeling three different types of tRNA-like oligos, we observed that RNA scaffolds can assemble and bring several short tRNA-acceptor-domain analogs, but not full-length tRNAs, to close proximity. Mg
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