Evidence map›Paper›PMID 22645361›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Domain activities of PapC usher reveal the mechanism of action of an Escherichia coli molecular machine.

Ender Volkan, Bradley A Ford, Jerome S Pinkner, Karen W Dodson, Nadine S Henderson, David G Thanassi, Gabriel Waksman, Scott J Hultgren

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Global redesign of a native β-barrel scaffold.Biochimica et biophysica acta · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Molecular basis of usher pore gating in Escherichia coli pilus biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Positively selected FimH residues enhance virulence during urinary tract infection by altering FimH conformation.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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.

Ender VolkanDepartment of Molecular Microbiology, Center for Women's Infectious Diseases Research, Washington University School of Medicine, St Louis, MO 63110, USA.
Bradley A Ford
Jerome S Pinkner
Karen W Dodson
Nadine S Henderson
David G Thanassi
Gabriel Waksman
Scott J Hultgren

Funding

Mechanism of the Usher in Assembly and Secretion of PiliR01GM062987 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI David G Thanassi · 2001 to 2026
$7.7M
CHAPERONE-ASSISTED PILI ASSEMBLY IN PATHOGENIC E. COLIR01AI029549 · NIAID · WASHINGTON UNIVERSITY · PI HULTGREN, SCOTT J., YUAN, PENG · 1991 to 2023
$5.7M
CHAPERONE ASSISTED PILI ASSEMBLY IN PATHOGENIC E COLIR37AI029549 · NIAID · WASHINGTON UNIVERSITY · PI HULTGREN, SCOTT J. · 1999 to 2008
$3.2M
STRUCTURAL GLYCOMICS OF THE E. COLI HOST-PATHOGEN INTERFACEK08DK093707 · NIDDK · WASHINGTON UNIVERSITY · PI FORD, BRADLEY A · 2012 to 2012
$141k
Medical Research Council G0800002NIAID NIH HHS AI049450NIAID NIH HHS R01 AI029549NIAID NIH HHS R37 AI029549NIDDK NIH HHS 1K08DK093707-01NIDDK NIH HHS K08 DK093707NIGMS NIH HHS R01 GM062987
6 · The paper itself

Abstract

P pili are prototypical chaperone-usher pathway-assembled pili used by Gram-negative bacteria to adhere to host tissues. The PapC usher contains five functional domains: a transmembrane β-barrel, a β-sandwich Plug, an N-terminal (periplasmic) domain (NTD), and two C-terminal (periplasmic) domains, CTD1 and CTD2. Here, we delineated usher domain interactions between themselves and with chaperone-subunit complexes and showed that overexpression of individual usher domains inhibits pilus assembly. Prior work revealed that the Plug domain occludes the pore of the transmembrane domain of a solitary usher, but the chaperone-adhesin-bound usher has its Plug displaced from the pore, adjacent to the NTD. We demonstrate an interaction between the NTD and Plug domains that suggests a biophysical basis for usher gating. Furthermore, we found that the NTD exhibits high-affinity binding to the chaperone-adhesin (PapDG) complex and low-affinity binding to the major tip subunit PapE (PapDE). We also demonstrate that CTD2 binds with lower affinity to all tested chaperone-subunit complexes except for the chaperone-terminator subunit (PapDH) and has a catalytic role in dissociating the NTD-PapDG complex, suggesting an interplay between recruitment to the NTD and transfer to CTD2 during pilus initiation. The Plug domain and the NTD-Plug complex bound all of the chaperone-subunit complexes tested including PapDH, suggesting that the Plug actively recruits chaperone-subunit complexes to the usher and is the sole recruiter of PapDH. Overall, our studies reveal the cooperative, active roles played by periplasmic domains of the usher to initiate, grow, and terminate a prototypical chaperone-usher pathway pilus.

Indexed as

BiophysicsCatalysisEscherichia coliEscherichia coli ProteinsMolecular ChaperonesPeriplasmPorinsatpG protein, E coliEscherichia coli ProteinsMolecular ChaperonesPorins

Identifiers

PMID22645361
PMCPMC3386062

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.