Evidence map›Paper›PMID 35137196›Full record

ArticleMolecular biology and evolution2022

In Vitro Evolution Reveals Noncationic Protein-RNA Interaction Mediated by Metal Ions.

Valerio G Giacobelli, Kosuke Fujishima, Martin Lepšík, Vyacheslav Tretyachenko, Tereza Kadavá, Mikhail Makarov, Lucie Bednárová, Petr Novák, Klára Hlouchová

Abstract read
In one paragraph

Article in Molecular biology and evolution, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Peptides En Route from Prebiotic to Biotic Catalysis.Accounts of chemical research · 2024
    Article
  11. The prebiotic emergence of biological evolution.Royal Society open science · 2024
    Article
  12. Biomacromolecules · 2024
    Article
  13. Review
  14. Article
  15. Article
  16. Peptide-RNA Coacervates as a Cradle for the Evolution of Folded Domains.Journal of the American Chemical Society · 2022
    Article
  17. Article
  18. Review
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Valerio G GiacobelliDepartment of Cell Biology, Faculty of Science, Charles University, BIOCEV, Prague, Czech Republic.
Kosuke FujishimaEarth-Life Science Institute, Tokyo Institute of Technology, Tokyo, Japan.
Martin LepšíkInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Prague, Czech Republic.
Vyacheslav TretyachenkoDepartment of Cell Biology, Faculty of Science, Charles University, BIOCEV, Prague, Czech Republic.
Tereza KadaváDepartment of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.
Mikhail MakarovDepartment of Cell Biology, Faculty of Science, Charles University, BIOCEV, Prague, Czech Republic.
Lucie BednárováInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Prague, Czech Republic.
Petr NovákInstitute of Microbiology, Czech Academy of Sciences, Vestec, Czech Republic.
Klára HlouchováDepartment of Cell Biology, Faculty of Science, Charles University, BIOCEV, Prague, Czech Republic.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA-peptide/protein interactions have been of utmost importance to life since its earliest forms, reaching even before the last universal common ancestor (LUCA). However, the ancient molecular mechanisms behind this key biological interaction remain enigmatic because extant RNA-protein interactions rely heavily on positively charged and aromatic amino acids that were absent (or heavily under-represented) in the early pre-LUCA evolutionary period. Here, an RNA-binding variant of the ribosomal uL11 C-terminal domain was selected from an approximately 1010 library of partially randomized sequences, all composed of ten prebiotically plausible canonical amino acids. The selected variant binds to the cognate RNA with a similar overall affinity although it is less structured in the unbound form than the wild-type protein domain. The variant complex association and dissociation are both slower than for the wild-type, implying different mechanistic processes involved. The profile of the wild-type and mutant complex stabilities along with molecular dynamics simulations uncovers qualitative differences in the interaction modes. In the absence of positively charged and aromatic residues, the mutant uL11 domain uses ion bridging (K+/Mg2+) interactions between the RNA sugar-phosphate backbone and glutamic acid residues as an alternative source of stabilization. This study presents experimental support to provide a new perspective on how early protein-RNA interactions evolved, where the lack of aromatic/basic residues may have been compensated by acidic residues plus metal ions.

Indexed as

Amino AcidsRNAIonsMolecular Dynamics SimulationAmino AcidsIonsRNAgenetic code evolutionmRNA-displayprotein evolutionRNA–protein interaction

Identifiers

PMID35137196
PMCPMC8892947

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Registered trials

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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.