Evidence map›Paper›PMID 24806796›Full record

ArticleMolecular microbiology2014

The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation in Pseudomonas aeruginosa.

Matthew A Jorgenson, Yan Chen, Atsushi Yahashiri, David L Popham, David S Weiss

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

88 citing papers in PubMed, 132 citations in OpenAlex.

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28 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Matthew A JorgensonDepartment of Microbiology, Carver College of Medicine, The University of Iowa, Iowa City, IA, 52242, USA.
Yan Chen
Atsushi Yahashiri
David L Popham
David S Weiss
University of Iowa · USVirginia Tech · US

Funding

Yerkes National Primate Research Center Role of type-I IFN in regulating COVID-19 induced inflammation and pathogenesisP51OD011132 · OD · EMORY UNIVERSITY · PI Joon Sup Lee · 2012 to 2026
$167.0M
Discovery and characterization of new bacterial cell division genesR01GM083975 · NIGMS · UNIVERSITY OF IOWA · PI WEISS, DAVID S · 2009 to 2012
$1.3M
Proteomic Analyses of Clostridium difficile Spore Germination ApparatusR21AI088298 · NIAID · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI HELM, RICHARD, JENSEN, RODERICK V · 2010 to 2011
$410k
NIAID NIH HHS R21 AI088298NIAID NIH HHS R21AI088298NIGMS NIH HHS GM083975NIGMS NIH HHS R01 GM083975NIH HHS P51 OD011132
6 · The paper itself

Abstract

Rare lipoprotein A (RlpA) is a widely conserved outer membrane protein of unknown function that has previously only been studied in Escherichia coli, where it localizes to the septal ring and scattered foci along the lateral wall, but mutants have no phenotypic change. Here we show rlpA mutants of Pseudomonas aeruginosa form chains of short, fat cells when grown in low osmotic strength media. These morphological defects indicate RlpA is needed for efficient separation of daughter cells and maintenance of rod shape. Analysis of peptidoglycan sacculi from an rlpA deletion mutant revealed increased tetra and hexasaccharides that lack stem peptides (hereafter called 'naked glycans'). Incubation of these sacculi with purified RlpA resulted in release of naked glycans containing 1,6-anhydro N-acetylmuramic acid ends. RlpA did not degrade sacculi from wild-type cells unless the sacculi were subjected to a limited digestion with an amidase to remove some of the stem peptides. Thus, RlpA is a lytic transglycosylase with a strong preference for naked glycan strands. We propose that RlpA activity is regulated in vivo by substrate availability, and that amidases and RlpA work in tandem to degrade peptidoglycan in the division septum and lateral wall.

Indexed as

Bacterial ProteinsCell DivisionCell WallGlycoside HydrolasesMutationPeptidoglycanPseudomonas aeruginosaSubstrate SpecificityBacterial ProteinsGlycoside HydrolasesPeptidoglycan

Identifiers

PMID24806796
PMCPMC4086221
OpenAlexW1960155418

What OpenQuestion holds

Textmetadata
LicenceTDM
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.