Journal article
The Bacterial Septal Ring Protein RlpA is a Lytic Transglycosylase that Contributes to Rod Shape and Daughter Cell Separation in Pseudomonas aeruginosa
Molecular microbiology, Vol.93(1), pp.113-128
07/2014
DOI: 10.1111/mmi.12643
PMCID: PMC4086221
PMID: 24806796
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.
Details
- Title: Subtitle
- The Bacterial Septal Ring Protein RlpA is a Lytic Transglycosylase that Contributes to Rod Shape and Daughter Cell Separation in Pseudomonas aeruginosa
- Creators
- Matthew A Jorgenson - Department of Biological Sciences Virginia Tech Blacksburg, VA 24061Yan Chen - Department of Biological Sciences Virginia Tech Blacksburg, VA 24061Atsushi Yahashiri - Department of Biological Sciences Virginia Tech Blacksburg, VA 24061David L Popham - Department of Biological Sciences Virginia Tech Blacksburg, VA 24061David S Weiss - Department of Biological Sciences Virginia Tech Blacksburg, VA 24061
- Resource Type
- Journal article
- Publication Details
- Molecular microbiology, Vol.93(1), pp.113-128
- DOI
- 10.1111/mmi.12643
- PMID
- 24806796
- PMCID
- PMC4086221
- ISSN
- 0950-382X
- eISSN
- 1365-2958
- Grant note
- DOI: 10.13039/100000002, name: National Institutes of Health, award: R01GM083975; DOI: 10.13039/100000002, name: National Institutes of Health, award: R21AI088298; DOI: 10.13039/100000001, name: National Science Foundation, award: DBI 7290775
- Language
- English
- Date published
- 07/2014
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984001218202771
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