The <scp>G</scp>ps<scp>B</scp> files: the truth is out there

Lewis, Richard J.

doi:10.1111/mmi.13612

Cited by 4 publications

(2 citation statements)

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“…Their identities are captured in imaginative cartoons suggesting the complexity of the protein-protein interaction network (Egan & Vollmer, 2013; Massidda et al , 2013; Szwedziak & Lowe, 2013; Fleurie et al , 2014; Egan & Vollmer, 2015; Leclercq et al , 2017; Lewis, 2017). A credible measure of the inchoate understanding of LT function is the absence of an LT in all of these cartoons.…”

Section: Resultsmentioning

confidence: 99%

Lytic transglycosylases: concinnity in concision of the bacterial cell wall

Dik

Marous

Fisher

et al. 2017

Critical Reviews in Biochemistry and Molecular Biology

138

188

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The lytic transglycosylases (LTs) are bacterial enzymes that catalyze the non-hydrolytic cleavage of the peptidoglycan structures of the bacterial cell wall. They are not catalysts of glycan synthesis as might be surmised from their name. Notwithstanding the seemingly mundane reaction catalyzed by the LTs, their lytic reactions serve bacteria for a series of astonishingly diverse purposes. These purposes include cell-wall synthesis, remodeling, and degradation; for the detection of cell-wall-acting antibiotics; for the expression of the mechanism of cell-wall-acting antibiotics; for the insertion of secretion systems and flagellar assemblies into the cell wall; as a virulence mechanism during infection by certain Gram-negative bacteria; and in the sporulation and germination of Gram-positive spores. Significant advances in the mechanistic understanding of each of these processes have coincided with the successive discovery of new LTs structures. In this review, we provide a systematic perspective on what is known on the structure-function correlations for the LTs, while simultaneously identifying numerous opportunities for the future study of these enigmatic enzymes.

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Section: Resultsmentioning

confidence: 99%

Lytic transglycosylases: concinnity in concision of the bacterial cell wall

Dik

Marous

Fisher

et al. 2017

Critical Reviews in Biochemistry and Molecular Biology

138

188

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“…A screen for gpsB suppressors in S. pneumoniae did not yield reoM mutations (and these strains do not contain reoY , consistent with a subordinate function for this gene), but instead suppressor mutations were found that affect phpP , which encodes a Ser/Thr protein phosphatase that acts in concert with StkP, the PASTA-eSTK of this organism (57, 58). Absence or inactivation of PhpP triggered an increase in StkP-dependent protein phosphorylation levels in the pneumococcus (57, 59).…”

Section: Discussionmentioning

confidence: 98%

PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM

Wamp

Rutter

Rismondo

et al. 2019

Preprint

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30Peptidoglycan (PG) is the main component of bacterial cell walls and the target for many 31 antibiotics. PG biosynthesis is tightly coordinated with cell wall growth and turnover and many 32 of these control activities depend upon PASTA-domain containing eukaryotic-like 33 serine/threonine protein kinases (PASTA-eSTK) that sense PG fragments. However, only a few 34 PG biosynthetic enzymes are actually direct kinase substrates. Here, we identify the conserved 35 ReoM protein as a novel PASTA-eSTK substrate in the Gram-positive pathogen Listeria 36 monocytogenes. Our data show that the phosphorylation of ReoM is essential as it controls 37 ClpCP-dependent proteolytic degradation of the essential enzyme MurA, which catalyses the first 38 committed step in PG biosynthesis. We also identify ReoY as a second novel factor required for 39 degradation of ClpCP substrates. Collectively, our data imply that the first committed step of PG 40 biosynthesis is activated through control of ClpCP protease activity in response to signals of PG 41 homeostasis imbalance.42 43 44 45The cell wall of Gram-positive bacteria is a complicated three-dimensional structure that engulfs 46 the cell as a closed sacculus. The main component of bacterial cell walls is peptidoglycan (PG), a 47 network of glycan strands crosslinked together by short peptides (1). PG biosynthesis starts with 48 the conversion of UDP-GlcNAc into lipid II, a disaccharide pentapeptide that is ligated to a 49 100 positive bacteria, which explains how PG biosynthesis is adjusted in these bacteria to meet PG 101 production and repair needs. 102 103 6 RESULTS 104 105Novel gpsB suppressor mutations in the lmo1503 (reoM) and lmo1921 (reoY) genes 106 A L. monocytogenes ΔgpsB mutant is unable to replicate at 42°C but forms suppressors 107 correcting this defect with high frequency (28). In a preliminary selection of gpsB suppressors, 108 the clpC and murZ genes, important for the stability of the UDP-N-acetylglucosamine 1-109 carboxyvinyltransferase MurA, were found to be mutated (28). We have characterized three more 110 shg (suppression of heat sensitive growth) suppressor mutants (shg8, shg10 and shg12) isolated 111 from a ΔgpsB mutant incubated on a BHI agar plate at 42°C. These three shg strains grew as fast 112 as the wild type when cultivated at 37°C or 42°C, whereas the parental ΔgpsB mutant grew at a 113 reduced rate at 37°C and did not grow at 42°C (Fig. 1A-B), as shown previously (32). 114Illumina sequencing of the shg8, shg10 and shg12 genomes identified one SNP in each strain that 115 was not found in the parental ΔgpsB strain. Strain shg8 carried a mutation in the uncharacterized 116 lmo1921 gene (herein named reoY, see below) that exchanged H87 into tyrosine; the same gene 117 was affected by the introduction of a premature stop codon after the 73 rd codon of reoY to yield 118 strain shg10. Strain shg12 carried a mutation in the ribosomal binding site (RBS) of the lmo1503 119 gene (renamed reoM), encoding another protein of unknown function and conta...

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