Evidence map›Paper›PMID 21784905›Full record

ArticleApplied and environmental microbiology2011

Unexpected stress-reducing effect of PhaP, a poly(3-hydroxybutyrate) granule-associated protein, in Escherichia coli.

Alejandra de Almeida, Mariela V Catone, Virgil A Rhodius, Carol A Gross, M Julia Pettinari

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

26 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Effect of SAM-Dependent Methyltransferases fromJournal of microbiology and biotechnology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Heterologous phasin expression inMetabolic engineering communications · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Understanding and engineering alcohol-tolerant bacteria using OMICS technology.World journal of microbiology & biotechnology · 2018
    Review
  17. Article
  18. Review
  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

5 authors at 3 institutions in 2 countries.

Alejandra de AlmeidaDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina.
Mariela V Catone
Virgil A Rhodius
Carol A Gross
M Julia Pettinari
Fundación Ciencias Exactas y Naturales · ARUniversity of California, San Francisco · USUniversity of Buenos Aires · AR

Funding

REGULATION OF THE HEAT-SHOCK RESPONSE IN E COLIR01GM036278 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI GROSS, CAROL ANNE · 1986 to 2016
$5.2M
REGULATION OF THE HEAT SHOCK RESPONSE IN E. COLIR37GM036278 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI GROSS, CAROL ANNE · 1995 to 2004
$2.0M
NIGMS NIH HHS GM036278NIGMS NIH HHS R01 GM036278NIGMS NIH HHS R37 GM036278
6 · The paper itself

Abstract

Phasins (PhaP) are proteins normally associated with granules of poly(3-hydroxybutyrate) (PHB), a biodegradable polymer accumulated by many bacteria as a reserve molecule. These proteins enhance growth and polymer production in natural and recombinant PHB producers. It has been shown that the production of PHB causes stress in recombinant Escherichia coli, revealed by an increase in the concentrations of several heat stress proteins. In this work, quantitative reverse transcription (qRT)-PCR analysis was used to study the effect of PHB accumulation, and that of PhaP from Azotobacter sp. strain FA8, on the expression of stress-related genes in PHB-producing E. coli. While PHB accumulation was found to increase the transcription of dnaK and ibpA, the expression of these genes and of groES, groEL, rpoH, dps, and yfiD was reduced, when PhaP was coexpressed, to levels even lower than those detected in the non-PHB-accumulating control. These results demonstrated the protective role of PhaP in PHB-synthesizing E. coli and linked the effects of the protein to the expression of stress-related genes, especially ibpA. The effect of PhaP was also analyzed in non-PHB-synthesizing strains, showing that expression of this heterologous protein has an unexpected protective effect in E. coli, under both normal and stress conditions, resulting in increased growth and higher resistance to both heat shock and superoxide stress by paraquat. In addition, PhaP expression was shown to reduce RpoH protein levels during heat shock, probably by reducing or titrating the levels of misfolded proteins.

Indexed as

Stress, PhysiologicalAzotobacterBacterial ProteinsDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGene Expression ProfilingHydroxybutyratesMolecular ChaperonesPolyestersPolyhydroxybutyratesRecombinant ProteinsBacterial ProteinsDNA-Binding ProteinsEscherichia coli ProteinsHydroxybutyratesMolecular ChaperonesPHAP protein, Bacteriapoly-beta-hydroxybutyratePolyestersPolyhydroxybutyratesRecombinant Proteins

Identifiers

PMID21784905
PMCPMC3187130
OpenAlexW2126920464

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.