Evidence map›Paper›PMID 21564339›Full record

ArticleMolecular microbiology2011

Mutations in the nucleotide binding pocket of MreB can alter cell curvature and polar morphology in Caulobacter.

Natalie A Dye, Zachary Pincus, Isabelle C Fisher, Lucy Shapiro, Julie A Theriot

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

36 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
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  15. Review
  16. Sizing up the bacterial cell cycle.Nature reviews. Microbiology · 2017
    Review
  17. Review
  18. Article
  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

5 authors at 3 institutions in 1 country.

Natalie A DyeDepartment of Biochemistry and Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA.
Zachary Pincus
Isabelle C Fisher
Lucy Shapiro
Julie A Theriot
Howard Hughes Medical Institute · USStanford University · USYale University · US

Funding

REGULATION OF DIFFERENTIATION IN CAULOBACTERR01GM032506 · NIGMS · YESHIVA UNIVERSITY · PI SHAPIRO, LUCILLE · 1985 to 2014
$7.1M
DEVELOPMENT CONTROL OF DNA REPLICATION IN CAULOBACTERR01GM051426 · NIGMS · STANFORD UNIVERSITY · PI SHAPIRO, LUCILLE · 1994 to 2013
$3.8M
MENINGOCOCCAL LIPOOLIGOSACCHARIDE &MUCOSAL PATHOGENESISR01AI033517 · NIAID · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 1993 to 2007
$1.7M
Surface protein dynamics in live bacterial pathogensR01AI067712 · NIAID · STANFORD UNIVERSITY · PI THERIOT, JULIE A. · 2006 to 2010
$1.5M
REGULATION OF DIFFERENTIATION IN CAULOBACTERR37GM032506 · NIGMS · STANFORD UNIVERSITY · PI SHAPIRO, LUCILLE · 1993 to 2002
$1.4M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI033517NIAID NIH HHS R01 AI067712NIAID NIH HHS R01 AI-33517NIAID NIH HHS R01 AI-67712NIGMS NIH HHS R01 GM032506NIGMS NIH HHS R01 GM051426NIGMS NIH HHS R01 GM32506NIGMS NIH HHS R01 GM51426NIGMS NIH HHS R37 GM032506
6 · The paper itself

Abstract

The maintenance of cell shape in Caulobacter crescentus requires the essential gene mreB, which encodes a member of the actin superfamily and the target of the antibiotic, A22. We isolated 35 unique A22-resistant Caulobacter strains with single amino acid substitutions near the nucleotide binding site of MreB. Mutations that alter cell curvature and mislocalize the intermediate filament crescentin cluster on the back surface of MreB's structure. Another subset have variable cell widths, with wide cell bodies and actively growing thin extensions of the cell poles that concentrate fluorescent MreB. We found that the extent to which MreB localization is perturbed is linearly correlated with the development of pointed cell poles and variable cell widths. Further, we find that a mutation to glycine of two conserved aspartic acid residues that are important for nucleotide hydrolysis in other members of the actin superfamily abolishes robust midcell recruitment of MreB but supports a normal rate of growth. These mutant strains provide novel insight into how MreB's protein structure, subcellular localization, and activity contribute to its function in bacterial cell shape.

Indexed as

Mutation, MissenseAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionAnti-Bacterial AgentsBacterial ProteinsCaulobacter crescentusCytoskeletal ProteinsDNA Mutational AnalysisMicroscopyModels, BiologicalModels, MolecularMolecular Sequence DataNucleotidesProtein BindingAnti-Bacterial AgentsBacterial ProteinsCytoskeletal ProteinsNucleotides

Identifiers

PMID21564339
PMCPMC3137890
OpenAlexW1873247595

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.