Evidence map›Paper›PMID 20212131›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Protein localization and dynamics within a bacterial organelle.

H Velocity Hughes, Edgar Huitema, Sean Pritchard, Kenneth C Keiler, Yves V Brun, Patrick H Viollier

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Dynamic translation regulation in Caulobacter cell cycle control.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. In-phase oscillation of global regulons is orchestrated by a pole-specific organizer.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Mechanisms of bacterial morphogenesis: evolutionary cell biology approaches provide new insights.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015
    Article
  17. Review
  18. Review
  19. 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

6 authors at 4 institutions in 2 countries.

H Velocity HughesDepartment of Biology, Indiana University, Bloomington, IN 47405, USA.
Edgar Huitema
Sean Pritchard
Kenneth C Keiler
Yves V Brun
Patrick H Viollier
Case Western Reserve University · USIndiana University Bloomington · USPennsylvania State University · USUniversity of Geneva · CH

Funding

GLOBAL CONTROL OF DIFFERENTIATION IN CAULOBACTERR01GM051986 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BRUN, YVES V · 1995 to 2016
$6.0M
The Role of tmRNA in development of C. crescentusR01GM068720 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI KEILER, KENNETH C · 2004 to 2014
$2.3M
NIGMS NIH HHS GM51986NIGMS NIH HHS R01 GM051986
6 · The paper itself

Abstract

Protein localization mechanisms dictate the functional and structural specialization of cells. Of the four polar surface organelles featured by the dimorphic bacterium Caulobacter crescentus, the stalk, a cylindrical extension of all cell envelope layers, is the least well characterized at the molecular level. Here we apply a powerful experimental scheme that integrates genetics with high-throughput localization to discover StpX, an uncharacterized bitopic membrane protein that modulates stalk elongation and is sequestered to the stalk. In stalkless mutants StpX is dispersed. Two populations of StpX were discernible within the stalk with different mobilities: an immobile one near the stalk base and a mobile one near the stalk tip. Molecular anatomy provides evidence that (i) the StpX transmembrane domain enables access to the stalk organelle, (ii) the N-terminal periplasmic domain mediates retention in the stalk, and (iii) the C-terminal cytoplasmic domain enhances diffusion within the stalk. Moreover, the accumulation of StpX and an N-terminally truncated isoform is differentially coordinated with the cell cycle. Thus, at the submicron scale the localization and the mobility of a protein are precisely regulated in space and time and are important for the correct organization of a subcellular compartment or organelle such as the stalk.

Indexed as

Bacterial ProteinsCaulobacter crescentusCell CycleCell Surface ExtensionsGenes, BacterialGreen Fluorescent ProteinsMembrane ProteinsMicroscopy, FluorescenceMutationProtein Structure, TertiaryRecombinant Fusion ProteinsBacterial ProteinsGreen Fluorescent ProteinsMembrane ProteinsRecombinant Fusion Proteins

Identifiers

PMID20212131
PMCPMC2851761
OpenAlexW2048577105

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.