ArticlePLoS biology2019
mRNA association by aminoacyl tRNA synthetase occurs at a putative anticodon mimic and autoregulates translation in response to tRNA levels.
Article in PLoS biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- RNA 5-methylcytosine marks mitochondrial double-stranded RNAs for degradation and cytosolic release.Molecular cell · 2024Article
- tRNA renovatio: Rebirth through fragmentation.Molecular cell · 2023Review
- Coordination of RNA modifications in the brain and beyond.Molecular psychiatry · 2023Review
- CDKAL1 Drives the Maintenance of Cancer Stem-Like Cells by Assembling the eIF4F Translation Initiation Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Article
- FMRP activity and control of Csw/SHP2 translation regulate MAPK-dependent synaptic transmission.PLoS biology · 2023Article
- A missense, loss-of-functionCold Spring Harbor molecular case studies · 2022Article
- Gain of C-Ala enables AlaRS to target the L-shaped tRNAAla.Nucleic acids research · 2022Article
- Human lysyl-tRNA synthetase evolves a dynamic structure that can be stabilized by forming complex.Cellular and molecular life sciences : CMLS · 2022Article
- Parameterising Translational Feedback Models of Autoregulatory RNA-Binding Proteins inMicroorganisms · 2022Article
- Biochemistry of Aminoacyl tRNA Synthetase and tRNAs and Their Engineering for Cell-Free and Synthetic Cell Applications.Frontiers in bioengineering and biotechnology · 2022Review
- Comprehensive characterization of mRNAs associated with yeast cytosolic aminoacyl-tRNA synthetases.RNA biology · 2021Article
- Review
- Mutually exclusive substrate selection strategy by human m3C RNA transferases METTL2A and METTL6.Nucleic acids research · 2021Article
- RNA modifications as a common denominator between tRNA and mRNA.Current genetics · 2021Review
- Discovery of 17 conserved structural RNAs in fungi.Nucleic acids research · 2021Article
- Pseudouridine-mediated translation control of mRNA by methionine aminoacyl tRNA synthetase.Nucleic acids research · 2021Article
- The Landscape of Aminoacyl-tRNA Synthetases Involved in Severe Acute Respiratory Syndrome Coronavirus 2 Infection.Frontiers in physiology · 2021Article
- Autoregulation of yeast ribosomal proteins discovered by efficient search for feedback regulation.Communications biology · 2020Article
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
Aminoacyl-tRNA synthetases (aaRSs) are well studied for their role in binding and charging tRNAs with cognate amino acids. Recent RNA interactome studies had suggested that these enzymes can also bind polyadenylated RNAs. Here, we explored the mRNA repertoire bound by several yeast aaRSs. RNA immunoprecipitation (RIP) followed by deep sequencing revealed unique sets of mRNAs bound by each aaRS. Interestingly, for every tested aaRSs, a preferential association with its own mRNA was observed, suggesting an autoregulatory process. Self-association of histidyl-tRNA synthetase (HisRS) was found to be mediated primarily through binding to a region predicted to fold into a tRNAHis anticodon-like structure. Introducing point mutations that are expected to disassemble this putative anticodon mimic alleviated self-association, concomitant with increased synthesis of the protein. Finally, we found that increased cellular levels of uncharged tRNAHis lead to reduced self-association and increased HisRS translation, in a manner that depends on the anticodon-like element. Together, these results reveal a novel post-transcriptional autoregulatory mechanism that exploits binding mimicry to control mRNA translation according to tRNA demands.
Indexed as
Identifiers
What OpenQuestion holds
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.