Evidence map›Paper›PMID 27603308›Full record

ArticlePloS one2016

Rhamnose Links Moonlighting Proteins to Membrane Phospholipid in Mycoplasmas.

James M Daubenspeck, Runhua Liu, Kevin Dybvig

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. T-DNA insertion mutagenesis inMicrobiology (Reading, England) · 2023
    Article
  4. Article
  5. Sequestration of a dual function DNA-binding protein byProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Protein moonlighting: what is it, and why is it important?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  15. Review
  16. Review
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 1 institution in 1 country.

James M DaubenspeckDepartment of Genetics, University of Alabama at Birmingham, Birmingham, Alabama, 35294, United States of America.
Runhua LiuDepartment of Genetics, University of Alabama at Birmingham, Birmingham, Alabama, 35294, United States of America.
Kevin DybvigDepartment of Genetics, University of Alabama at Birmingham, Birmingham, Alabama, 35294, United States of America.
University of Alabama at Birmingham · US

Funding

Mechanisms of Mycoplasmal Disease PathogenesisR01AI063909 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DYBVIG, KEVIN F · 2005 to 2014
$3.0M
NIAID NIH HHS R01 AI063909
6 · The paper itself

Abstract

Many proteins that have a primary function as a cytoplasmic protein are known to have the ability to moonlight on the surface of nearly all organisms. An example is the glycolytic enzyme enolase, which can be found on the surface of many types of cells from bacteria to human. Surface enolase is not enzymatic because it is monomeric and oligomerization is required for glycolytic activity. It can bind various molecules and activate plasminogen. Enolase lacks a signal peptide and the mechanism by which it attaches to the surface is unknown. We found that treatment of whole cells of the murine pathogen Mycoplasma pulmonis with phospholipase D released enolase and other common moonlighting proteins. Glycostaining suggested that the released proteins were glycosylated. Cytoplasmic and membrane-bound enolase was isolated by immunoprecipitation. No post-translational modification was detected on cytoplasmic enolase, but membrane enolase was associated with lipid, phosphate and rhamnose. Treatment with phospholipase released the lipid and phosphate from enolase but not the rhamnose. The site of rhamnosylation was identified as a glutamine residue near the C-terminus of the protein. Rhamnose has been found in all species of mycoplasma examined but its function was previously unknown. Mycoplasmas are small bacteria with have no peptidoglycan, and rhamnose in these organisms is also not associated with polysaccharide. We suggest that rhamnose has a central role in anchoring proteins to the membrane by linkage to phospholipid, which may be a general mechanism for the membrane association of moonlighting proteins in mycoplasmas and perhaps other bacteria.

Indexed as

Amino Acid SequenceBacterial ProteinsCell MembraneChromatography, High Pressure LiquidElectrophoresis, Polyacrylamide GelGas Chromatography-Mass SpectrometryMembrane ProteinsMycoplasmaPeptidesPhospholipase DPhospholipidsPhosphopyruvate HydrataseProtein Processing, Post-TranslationalReference StandardsRhamnoseTandem Mass SpectrometryBacterial ProteinsMembrane ProteinsPeptidesPhospholipase DPhospholipidsPhosphopyruvate HydrataseRhamnose

Identifiers

PMID27603308
PMCPMC5014317
OpenAlexW2517911695

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.