Evidence map›Paper›PMID 29109287›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

Yunfeng Gao, Yong Hwee Foo, Ricksen S Winardhi, Qingnan Tang, Jie Yan, Linda J Kenney

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Advancing evolution: Bacteria break down gene silencer to express horizontally acquired genes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

6 authors.

Yunfeng GaoMechanobiology Institute, National University of Singapore, Singapore 117411.
Yong Hwee FooMechanobiology Institute, National University of Singapore, Singapore 117411.
Ricksen S WinardhiDepartment of Physics, National University of Singapore, Singapore 117411.
Qingnan TangDepartment of Physics, National University of Singapore, Singapore 117411.
Jie YanMechanobiology Institute, National University of Singapore, Singapore 117411.
Linda J KenneyMechanobiology Institute, National University of Singapore, Singapore 117411; kenneyl@uic.edu.ORCID 0000-0002-8658-0717

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleoid-associated proteins (NAPs) facilitate chromosome organization in bacteria, but the precise mechanism remains elusive. H-NS is a NAP that also plays a major role in silencing pathogen genes. We used genetics, single-particle tracking in live cells, superresolution microscopy, atomic force microscopy, and molecular dynamics simulations to examine H-NS/DNA interactions in single cells. We discovered a role for the unstructured linker region connecting the N-terminal oligomerization and C-terminal DNA binding domains. In the present work we demonstrate that linker amino acids promote engagement with DNA. In the absence of linker contacts, H-NS binding is significantly reduced, although no change in chromosome compaction is observed. H-NS is not localized to two distinct foci; rather, it is scattered all around the nucleoid. The linker makes DNA contacts that are required for gene silencing, while chromosome compaction does not appear to be an important H-NS function.

Indexed as

Gene Expression Regulation, BacterialGene SilencingAmino Acid SequenceBinding SitesDNAEscherichia coliEscherichia coli ProteinsFimbriae ProteinsHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular Dynamics SimulationProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsSequence AlignmentDNAEscherichia coli ProteinsFimbriae ProteinsFimG protein, E coliatomic force microscopyH-NSnucleoid-associated proteinssingle-particle trackingsuperresolution microscopy

Identifiers

PMID29109287
PMCPMC5703333

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.