ArticleRNA (New York, N.Y.)2001
A minihelix-loop RNA acts as a trans-aminoacylation catalyst.
Article in RNA (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Reprogramming the genetic code with flexizymes.Nature reviews. Chemistry · 2024Review
- An anticodon-sensing T-boxzyme generates the elongator nonproteinogenic aminoacyl-tRNA in situ of a custom-made translation system for incorporation.Nucleic acids research · 2024Article
- Cell-free Biosynthesis of Peptidomimetics.Biotechnology and bioprocess engineering : BBE · 2023Review
- Coevolution Theory of the Genetic Code at Age Forty: Pathway to Translation and Synthetic Life.Life (Basel, Switzerland) · 2016Article
- Landmarks in the Evolution of (t)-RNAs from the Origin of Life up to Their Present Role in Human Cognition.Life (Basel, Switzerland) · 2015Review
- Evolutionary routes from a prebiotic ANA-world.Communicative & integrative biology · 2012Article
- The scenario on the origin of translation in the RNA world: in principle of replication parsimony.Biology direct · 2010Article
- Multiple translational products from a five-nucleotide ribozyme.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Minihelix-loop RNAs: minimal structures for aminoacylation catalysts.Nucleic acids research · 2002Article
- Concurrent molecular recognition of the amino acid and tRNA by a ribozyme.RNA (New York, N.Y.) · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We previously reported a bifunctional ribozyme that catalyzes self-aminoacylation and subsequent acyl-transfer to a tRNA. The ribozyme selectively recognizes a biotinyl-glutamine substrate, and charges the tRNA molecule in trans. Structurally, there are two catalytic domains, referred to as glutamine-recognition (QR) and acyl-transferase (ATRib). We report here the essential catalytic core of the QR domain as determined by extensive biochemical probing, mutation, and structural minimization. The minimal core of the QR domain is a 29-nt helix-loop RNA, which is also able to glutaminylate ATRib in trans. Its amino acid binding site is embedded in an 11-nt cluster that is adjacent to the loop that interacts with the ATRib domain. Our study shows that a minihelix-loop RNA can act as a trans-aminoacylation catalyst, which lends support for the critical role of minihelix-loops in the early evolution of the aminoacylation system.
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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.