Evidence map›Paper›PMID 17573816›Full record

ArticleMolecular microbiology2007

An atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS.

James S Fraser, John P Merlie, Nathaniel Echols, Shellie R Weisfield, Tâm Mignot, David E Wemmer, David R Zusman, Tom Alber

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

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  20. Gliding motility revisited: how do the myxobacteria move without flagella?Microbiology and molecular biology reviews : MMBR · 2010
    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

8 authors at 3 institutions in 2 countries.

James S FraserDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3320, USA.
John P Merlie
Nathaniel Echols
Shellie R Weisfield
Tâm Mignot
David E Wemmer
David R Zusman
Tom Alber
University of California, Berkeley · USCentre National de la Recherche Scientifique · FRLawrence Berkeley National Laboratory · US

Funding

SENSORY TRANSDUCTION AND DEVELOPMENT IN A BACTERIUMR01GM020509 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ZUSMAN, DAVID ROBERT · 1985 to 2014
$5.9M
Structural Studies of the Bacterial Transcription Factor NtrCR01GM062163 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI WEMMER, DAVID E · 2001 to 2014
$3.1M
X-RAY STRUCTURE AND STABILITY OF THE LEUCINE ZIPPERR01GM048958 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ALBER, THOMAS C · 1992 to 2008
$2.8M
NIGMS NIH HHS GM20509NIGMS NIH HHS GM62163NIGMS NIH HHS R01 GM020509NIGMS NIH HHS R01 GM048958NIGMS NIH HHS R01 GM062163
6 · The paper itself

Abstract

The Myxococcus xanthus FrzS protein transits from pole-to-pole within the cell, accumulating at the pole that defines the direction of movement in social (S) motility. Here we show using atomic-resolution crystallography and NMR that the FrzS receiver domain (RD) displays the conserved switch Tyr102 in an unusual conformation, lacks the conserved Asp phosphorylation site, and fails to bind Mg(2+) or the phosphoryl analogue, Mg(2+) x BeF(3). Mutation of Asp55, closest to the canonical site of RD phosphorylation, showed no motility phenotype in vivo, demonstrating that phosphorylation at this site is not necessary for domain function. In contrast, the Tyr102Ala and His92Phe substitutions on the canonical output face of the FrzS RD abolished S-motility in vivo. Single-cell fluorescence microscopy measurements revealed a striking mislocalization of these mutant FrzS proteins to the trailing cell pole in vivo. The crystal structures of the mutants suggested that the observed conformation of Tyr102 in the wild-type FrzS RD is not sufficient for function. These results support the model that FrzS contains a novel 'pseudo-receiver domain' whose function requires recognition of the RD output face but not Asp phosphorylation.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAspartic AcidBacterial ProteinsConserved SequenceCrystallographyHistidineMagnesiumMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMolecular Sequence DataMutationMyxococcus xanthusPhosphorylationProtein Structure, SecondaryProtein Structure, TertiaryAspartic AcidBacterial ProteinsFrzS protein, Myxococcus xanthusHistidineMagnesiumMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsTyrosine

Identifiers

PMID17573816
PMCPMC1974792
OpenAlexW2125009011

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.