Evidence map›Paper›PMID 39557413›Full record

ArticleNucleic acids research2024

Profiling of i-motif-binding proteins reveals functional roles of nucleolin in regulation of high-order DNA structures.

Yuki Ban, Yuka Ando, Yuma Terai, Risa Matsumura, Keita Nakane, Shigenori Iwai, Shinichi Sato, Junpei Yamamoto

Abstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
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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

8 authors.

Yuki BanDivision of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Yuka AndoDivision of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Yuma TeraiDivision of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Risa MatsumuraDivision of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Keita NakaneFrontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3 Aramaki aza-Aoba, Aoba-ku, Sendai, Miyagi 980-8578, Japan.
Shigenori IwaiDivision of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Shinichi SatoFrontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3 Aramaki aza-Aoba, Aoba-ku, Sendai, Miyagi 980-8578, Japan.
Junpei YamamotoDivision of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.ORCID 0000-0002-5036-991X

Funding

Japan Society for the Promotion of Science 21H05503JSPS FellowshipJST FOREST JPMJFR2005Sunbor ScholarshipTakeda Science FoundationThe Uehara Memorial Foundation
6 · The paper itself

Abstract

Non-canonical DNA structures, such as the G-quadruplex (G4) and i-motif (iM), are formed at guanine- and cytosine-rich sequences, respectively, in living cells and involved in regulating various biological processes during the cell cycle. Therefore, the formation and resolution of these non-canonical structures must be dynamically regulated by physiological conditions or factors that can bind G4 and iM structures. Although many G4 binding proteins responsible for tuning the G4 structure have been discovered, the structural regulation of iM by iM-binding proteins remains enigmatic. In this study, we developed a protein-labeling DNA probe bearing an alkyne moiety through a reactive linker, for proximity-labeling of nucleic acid-binding proteins, and searched for new iM-binding proteins. Alkyne-modified proteins in the nuclear extract of HeLa cells were labeled with biotin via a click reaction and then captured with streptavidin-coated magnetic beads. This fingerprint-targeting enrichment, followed by proteome analyses, identified new candidate proteins that potentially bind to the iM structure, in addition to the reported iM-binding proteins. Among the newly identified candidates, we characterized a nucleolar protein, nucleolin, that binds to the iM structure and relaxes it, while nucleolin stabilizes the G4 structure.

Indexed as

DNADNA-Binding ProteinsG-QuadruplexesNucleolinPhosphoproteinsRNA-Binding ProteinsHeLa CellsHumansNucleotide MotifsProtein BindingDNADNA-Binding ProteinsNucleolinPhosphoproteinsRNA-Binding Proteins

Identifiers

PMID39557413
PMCPMC11662649

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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.