Evidence map›Paper›PMID 17605819›Full record

ArticleBMC microbiology2007

Mapping phosphoproteins in Mycoplasma genitalium and Mycoplasma pneumoniae.

Hsun-Cheng Su, Clyde A Hutchison, Morgan C Giddings

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

18 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Frontiers in veterinary science · 2023
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

3 authors at 3 institutions in 1 country.

Hsun-Cheng SuDepartment of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. seansu@email.unc.edu <seansu@email.unc.edu>
Clyde A Hutchison
Morgan C Giddings
J. Craig Venter Institute · USNorth Carolina State University · USUniversity of North Carolina at Chapel Hill · US

Funding

Software to Identify Post-translational Modifications From Proteomic Data SetsR01RR020823 · NCRR · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GIDDINGS, MORGAN CORINNE · 2004 to 2011
$2.6M
NCRR NIH HHS R01 RR020823
6 · The paper itself

Abstract

backgroundLittle is known regarding the extent or targets of phosphorylation in mycoplasmas, yet in many other bacterial species phosphorylation is known to play an important role in signaling and regulation of cellular processes. To determine the prevalence of phosphorylation in mycoplasmas, we examined the CHAPS-soluble protein fractions of Mycoplasma genitalium and Mycoplasma pneumoniae by two-dimensional gel electrophoresis (2-DE), using a combination of Pro-Q Diamond phosphoprotein stain and 33P labeling. Protein spots that were positive for phosphorylation were identified by peptide mass fingerprinting using MALDI-TOF-TOF mass spectrometry.

resultsWe identified a total of 24 distinct phosphoproteins, about 3% and 5% of the total protein complement in M. pneumoniae and M. genitalium, respectively, indicating that phosphorylation occurs with prevalence similar to many other bacterial species. Identified phosphoproteins include pyruvate dehydrogenase E1 alpha and beta subunits, enolase, heat shock proteins DnaK and GroEL, elongation factor Tu, cytadherence accessory protein HMW3, P65, and several hypothetical proteins. These proteins are involved in energy metabolism, carbohydrate metabolism, translation/transcription and cytadherence. Interestingly, fourteen of the 24 phosphoproteins we identified (58%) were previously reported as putatively associated with a cytoskeleton-like structure that is present in the mycoplasmas, indicating a potential regulatory role for phosphorylation in this structure.

conclusionThis study has shown that phosphorylation in mycoplasmas is comparable to that of other bacterial species. Our evidence supports a link between phosphorylation and cytadherence and/or a cytoskeleton-like structure, since over half of the proteins identified as phosphorylated have been previously associated with these functions. This opens the door to further research into the purposes and mechanisms of phosphorylation for mycoplasmas.

Indexed as

Bacterial ProteinsCarbohydrate MetabolismElectrophoresis, Gel, Two-DimensionalEnergy MetabolismMycoplasma genitaliumPeptide Elongation Factor TuPeptide MappingPhosphoproteinsPhosphopyruvate HydratasePhosphorylationPneumonia, MycoplasmaProteomicsPyruvate Dehydrogenase (Lipoamide)Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationBacterial ProteinsPeptide Elongation Factor TuPhosphoproteinsPhosphopyruvate Hydratasepyruvate dehydrogenase E1alpha subunitpyruvate dehydrogenase E1 beta subunitPyruvate Dehydrogenase (Lipoamide)

Identifiers

PMID17605819
PMCPMC1947986
OpenAlexW2142536772

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.