Evidence map›Paper›PMID 24118129›Full record

ArticleMolecular microbiology2013

Co-ordinate synthesis and protein localization in a bacterial organelle by the action of a penicillin-binding-protein.

H Velocity Hughes, John P Lisher, Gail G Hardy, David T Kysela, Randy J Arnold, David P Giedroc, Yves V Brun

Abstract read
In one paragraph

Article in Molecular microbiology, 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
–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

18 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
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  13. β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. Review
  16. Article
  17. Manganese acquisition and homeostasis at the host-pathogen interface.Frontiers in cellular and infection microbiology · 2013
    Review
  18. 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

7 authors.

H Velocity HughesDepartment of Biology, Indiana University, Bloomington, IN, 47405, USA.
John P Lisher
Gail G Hardy
David T Kysela
Randy J Arnold
David P Giedroc
Yves V Brun

Funding

GLOBAL CONTROL OF DIFFERENTIATION IN CAULOBACTERR01GM051986 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BRUN, YVES V · 1995 to 2016
$6.0M
ZINC COORDINATION AND REGULATION OF ZINC METALLOPROTEINSR01GM042569 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI GIEDROC, DAVID P. · 1996 to 2015
$4.9M
ZINC DOMAIN STRUCTURE AND FUNCTION IN T4 GENE 32 PROTEINR29GM042569 · NIGMS · TEXAS AGRILIFE RESEARCH · PI GIEDROC, DAVID P. · 1991 to 1995
–
NIGMS NIH HHS GM042569NIGMS NIH HHS GM051986NIGMS NIH HHS R01 GM042569NIGMS NIH HHS R01 GM051986
6 · The paper itself

Abstract

Organelles with specialized form and function occur in diverse bacteria. Within the Alphaproteobacteria, several species extrude thin cellular appendages known as stalks, which function in nutrient uptake, buoyancy and reproduction. Consistent with their specialization, stalks maintain a unique molecular composition compared with the cell body, but how this is achieved remains to be fully elucidated. Here we dissect the mechanism of localization of StpX, a stalk-specific protein in Caulobacter crescentus. Using a forward genetics approach, we identify a penicillin-binding-protein, PbpC, which is required for the localization of StpX in the stalk. We show that PbpC acts at the stalked cell pole to anchor StpX to rigid components of the outer membrane of the elongating stalk, concurrent with stalk synthesis. Stalk-localized StpX in turn functions in cellular responses to copper and zinc, suggesting that the stalk may contribute to metal homeostasis in Caulobacter. Together, these results identify a novel role for a penicillin-binding-protein in compartmentalizing a bacterial organelle it itself helps create, raising the possibility that cell wall-synthetic enzymes may broadly serve not only to synthesize the diverse shapes of bacteria, but also to functionalize them at the molecular level.

Indexed as

Bacterial ProteinsCaulobacter crescentusCopperGenes, BacterialGreen Fluorescent ProteinsHomeostasisMembrane ProteinsMicroscopy, FluorescenceOrganellesPenicillin-Binding ProteinsProtein TransportZincBacterial ProteinsCopperGreen Fluorescent ProteinsMembrane ProteinsPenicillin-Binding ProteinsZinc

Identifiers

PMID24118129
PMCPMC3864544

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Registered trials

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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.