Evidence map›Paper›PMID 15995210›Full record

ArticleJournal of bacteriology2005

Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.

Lucia Musumeci, Cristina Bongiorni, Lutz Tautz, Robert A Edwards, Andrei Osterman, Marta Perego, Tomas Mustelin, Nunzio Bottini

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 2005. 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 25% 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, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Widespread Arginine Phosphorylation in Staphylococcus aureus.Molecular & cellular proteomics : MCP · 2022
    Article
  5. Article
  6. Quantitative proteomic reveals gallium maltolate induces an iron-limited stress response and reduced quorum-sensing in Pseudomonas aeruginosa.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  7. Spectral Library Based Analysis of Arginine Phosphorylations inMolecular & cellular proteomics : MCP · 2018
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

8 authors at 2 institutions in 1 country.

Lucia MusumeciThe Institute for Genetic Medicine, University of Southern California, Los Angeles, 90033, USA.
Cristina Bongiorni
Lutz Tautz
Robert A Edwards
Andrei Osterman
Marta Perego
Tomas Mustelin
Nunzio Bottini
Sanford Burnham Prebys Medical Discovery Institute · USScripps Research Institute · US

Funding

Protein Aspartate Phosphatases in DevelopmentR01GM055594 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI PEREGO, MARTA · 1998 to 2006
$2.7M
NIGMS NIH HHS GM55594NIGMS NIH HHS R01 GM055594
6 · The paper itself

Abstract

In gram-negative organisms, enzymes belonging to the low-molecular-weight protein tyrosine phosphatase (LMPTP) family are involved in the regulation of important physiological functions, including stress resistance and synthesis of the polysaccharide capsule. LMPTPs have been identified also in gram-positive bacteria, but their functions in these organisms are presently unknown. We cloned two putative LMPTPs from Bacillus subtilis, YfkJ and YwlE, which are highly similar to each other in primary structure as well as to LMPTPs from gram-negative bacteria. When purified from overexpressing Escherichia coli strains, both enzymes were able to dephosphorylate p-nitrophenyl-phosphate and phosphotyrosine-containing substrates in vitro but showed significant differences in kinetic parameters and sensitivity to inhibitors. Transcriptional analyses showed that yfkJ was transcribed at a low level throughout the growth cycle and underwent a sigma(B)-dependent transcriptional upregulation in response to ethanol stress. The transcription of ywlE was growth dependent but stress insensitive. Genomic deletion of each phosphatase-encoding gene led to a phenotype of reduced bacterial resistance to ethanol stress, which was more marked in the ywlE deletion strain. Our study suggests that YfkJ and YwlE play roles in B. subtilis stress resistance.

Indexed as

Amino Acid SequenceBacillus subtilisBase SequenceCations, DivalentComputational BiologyConserved SequenceDNA PrimersEscherichia coliHumansKineticsMolecular Sequence DataMolecular WeightProtein Tyrosine PhosphatasesRestriction MappingReverse Transcriptase Polymerase Chain ReactionSequence AlignmentCations, DivalentDNA PrimersProtein Tyrosine Phosphatases

Identifiers

PMID15995210
PMCPMC1169535
OpenAlexW2146063485

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.