Evidence map›Paper›PMID 35435704›Full record

ArticlemBio2022

The Histone H1-Like Protein AlgP Facilitates Even Spacing of Polyphosphate Granules in Pseudomonas aeruginosa.

Ravi Chawla, Steven Klupt, Vadim Patsalo, James R Williamson, Lisa R Racki

Open access · goldAbstract read
In one paragraph

Article in mBio, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. A bacterial translation activator with an intrinsically disordered RNA-binding region.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. The Protein Scaffolding Functions of Polyphosphate.Journal of molecular biology · 2024
    Review
  11. Article
  12. Polyphosphate affects cytoplasmic and chromosomal dynamics in nitrogen-starvedProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Review
  14. Reentrant DNA shells tune polyphosphate condensate size.bioRxiv : the preprint server for biology · 2023
    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

5 authors at 1 institution in 1 country.

Ravi Chawla *Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, California, USA.ORCID 0000-0003-1867-9528
Steven Klupt *Department of Immunology and Microbiology, Scripps Research, La Jolla, California, USA.
Vadim PatsaloDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, California, USA.ORCID 0000-0001-6047-5858
James R WilliamsonDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, California, USA.ORCID 0000-0002-8772-468X
Lisa R RackiDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, California, USA.ORCID 0000-0003-2209-7301
Scripps Institution of Oceanography · US

Funding

Dynamics of the Bacterial Ribosome and Proteome (Equipment Supplement)R35GM136412 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI James R Williamson · 2020 to 2026
$4.9M
NIGMS NIH HHS R35 GM136412
6 · The paper itself

Abstract

Synthesis of polyphosphate (polyP) is an ancient and universal stress and starvation response in bacteria. In many bacteria, polyP chains come together to form granular superstructures within cells. Some species appear to regulate polyP granule subcellular organization. Despite the critical role of polyP in starvation fitness, the composition of these structures, mechanism(s) underpinning their organization, and functional significance of such organization are poorly understood. We previously determined that granules become transiently evenly spaced on the cell's long axis during nitrogen starvation in the opportunistic human pathogen Pseudomonas aeruginosa. Here, we developed a granule-enrichment protocol to screen for polyP granule-localizing proteins. We identified AlgP as a protein that associates with polyP granules. We further discovered that AlgP is required for the even spacing of polyP granules. AlgP is a DNA-binding protein with a 154 amino acid C-terminal domain enriched in "KPAA" repeats and variants of this repeat, with an overall sequence composition similar to the C-terminal tail of eukaryotic histone H1. Granule size, number, and spacing are significantly perturbed in the absence of AlgP, or when AlgP is truncated to remove the C-terminus. The

Indexed as

Bacterial ProteinsDNA-Binding ProteinsPolyphosphatesPseudomonas aeruginosaTranscription FactorsAlginatesHistonesAlginatesalgP protein, Pseudomonas aeruginosaBacterial ProteinsDNA-Binding ProteinsHistonesPolyphosphatesTranscription FactorsAlgPcell biologypolyphosphatepseudomonas aeruginosastarvation

Identifiers

PMID35435704
PMCPMC9239181
OpenAlexW4226040427

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.