Evidence map›Paper›PMID 23828892›Full record

ArticleMolecular & cellular proteomics : MCP2013

Phosphoproteomic analysis reveals the effects of PilF phosphorylation on type IV pilus and biofilm formation in Thermus thermophilus HB27.

Wan-Ling Wu, Jiahn-Haur Liao, Guang-Huey Lin, Miao-Hsia Lin, Ying-Che Chang, Suh-Yuen Liang, Feng-Ling Yang, Kay-Hooi Khoo, Shih-Hsiung Wu

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. 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
1.5field-weighted citation impact, top 18% 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, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Goals and Challenges in Bacterial Phosphoproteomics.International journal of molecular sciences · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. New Technologies for Studying Biofilms.Microbiology spectrum · 2015
    Review
  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

9 authors at 3 institutions in 1 country.

Wan-Ling WuInstitute of Biochemical Sciences, College of Life Sciences, National Taiwan University, Taipei 106, Taiwan;
Jiahn-Haur Liao
Guang-Huey Lin
Miao-Hsia Lin
Ying-Che Chang
Suh-Yuen Liang
Feng-Ling Yang
Kay-Hooi Khoo
Shih-Hsiung Wu
Institute of Biological Chemistry, Academia Sinica · TWAcademia Sinica · TWTzu Chi University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thermus thermophilus HB27 is an extremely thermophilic eubacteria with a high frequency of natural competence. This organism is therefore often used as a thermophilic model to investigate the molecular basis of type IV pili-mediated functions, such as the uptake of free DNA, adhesion, twitching motility, and biofilm formation, in hot environments. In this study, the phosphoproteome of T. thermophilus HB27 was analyzed via a shotgun approach and high-accuracy mass spectrometry. Ninety-three unique phosphopeptides, including 67 in vivo phosphorylated sites on 53 phosphoproteins, were identified. The distribution of Ser/Thr/Tyr phosphorylation sites was 57%/36%/7%. The phosphoproteins were mostly involved in central metabolic pathways and protein/cell envelope biosynthesis. According to this analysis, the ATPase motor PilF, a type IV pili-related component, was first found to be phosphorylated on Thr-368 and Ser-372. Through the point mutation of PilF, mimic phosphorylated mutants T368D and S372E resulted in nonpiliated and nontwitching phenotypes, whereas nonphosphorylated mutants T368V and S372A displayed piliation and twitching motility. In addition, mimic phosphorylated mutants showed elevated biofilm-forming abilities with a higher initial attachment rate, caused by increasing exopolysaccharide production. In summary, the phosphorylation of PilF might regulate the pili and biofilm formation associated with exopolysaccharide production.

Indexed as

BiofilmsBiopolymersEscherichia coliFimbriae, BacterialFimbriae ProteinsPhosphopeptidesPhosphoproteinsPhosphorylationPolysaccharidesProteomicsThermus thermophilusBiopolymersFimbriae ProteinsPhosphopeptidesPhosphoproteinsPolysaccharides

Identifiers

PMID23828892
PMCPMC3790284
OpenAlexW2107832932

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.