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PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM

ABSTRACT: PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM

PROVIDER: PRJEB35110 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR3624954_1.fastq.gz	Fastqsanger.gz
	ERR3624954_2.fastq.gz	Fastqsanger.gz
	ERR3624955_1.fastq.gz	Fastqsanger.gz
	ERR3624955_2.fastq.gz	Fastqsanger.gz
	ERR3624956_1.fastq.gz	Fastqsanger.gz

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PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM.

Project description:Peptidoglycan (PG) is the main component of bacterial cell walls and the target for many antibiotics. PG biosynthesis is tightly coordinated with cell wall growth and turnover, and many of these control activities depend upon PASTA-domain containing eukaryotic-like serine/threonine protein kinases (PASTA-eSTK) that sense PG fragments. However, only a few PG biosynthetic enzymes are direct kinase substrates. Here, we identify the conserved ReoM protein as a novel PASTA-eSTK substrate in the Gram-positive pathogen Listeria monocytogenes. Our data show that the phosphorylation of ReoM is essential as it controls ClpCP-dependent proteolytic degradation of the essential enzyme MurA, which catalyses the first committed step in PG biosynthesis. We also identify ReoY as a second novel factor required for degradation of ClpCP substrates. Collectively, our data imply that the first committed step of PG biosynthesis is activated through control of ClpCP protease activity in response to signals of PG homeostasis imbalance.

| S-EPMC7286690 | biostudies-literature

MurA escape mutations uncouple peptidoglycan biosynthesis from PrkA signaling

Project description:MurA escape mutations uncouple peptidoglycan biosynthesis from PrkA signaling

| PRJEB47255 | ENA

Cdk1-dependent phosphorylation of Clr4Suv39H controls a histone H3 methylation switch that is essential for gametogenesis

Project description:Cdk1-dependent phosphorylation of Clr4Suv39H controls a histone H3 methylation switch that is essential for gametogenesis

| PRJNA755592 | ENA

MtrA regulation of essential peptidoglycan cleavage in Mycobacterium tuberculosis during infection [mtrA_knockdown]

Project description:MtrA regulation of essential peptidoglycan cleavage in Mycobacterium tuberculosis during infection [mtrA_knockdown]

| PRJNA702058 | ENA

MtrA regulation of essential peptidoglycan cleavage in Mycobacterium tuberculosis during infection [pH]

Project description:MtrA regulation of essential peptidoglycan cleavage in Mycobacterium tuberculosis during infection [pH]

| PRJNA694847 | ENA

MtrA regulation of essential peptidoglycan cleavage in Mycobacterium tuberculosis during infection [MtrA_OE_pH]

Project description:MtrA regulation of essential peptidoglycan cleavage in Mycobacterium tuberculosis during infection [MtrA_OE_pH]

| PRJNA702057 | ENA

MtrA regulation of essential peptidoglycan cleavage in Mycobacterium tuberculosis during infection [mtrA_knockdown]

Project description:The success of Mycobacterium tuberculosis (Mtb) is largely due to its ability to withstand numerous stresses imposed by host immunity. Here, we present a data-driven model that captures these adaptive mechanisms and reveals the dynamic interplay of host-derived stresses and genome-encoded regulatory programs in Mtb. The model captures the genome-wide distribution of cis-acting gene regulatory elements and the conditional influences of transcription factors at those elements to elicit environment-specific responses. Analysis of transcriptional responses that may be essential for Mtb’s survival in acidic conditions identified regulatory control by the MtrAB two-component signal system. Using genome-wide transcriptomics as well as imaging studies, we have characterized the MtrAB circuit by tunable CRISPRi knockdown in both Mtb and the non-pathogenic organism, M. smegmatis (Msm). These experiments validated the essentiality of MtrA in Mtb, but not Msm. We identified that MtrA regulates multiple enzymes that cleave cell wall peptidoglycan and is required for efficient cell division. Moreover, our results suggest that peptidoglycan cleavage, regulated by MtrA, is required for Mtb to survive intracellular stress. Further, we present MtrA as an attractive drug target, as even weak repression of mtrA results in loss of Mtb viability and completely clears the bacteria with low-dose isoniazid or rifampicin treatment.

2021-07-16 | GSE166805 | GEO

MtrA regulation of essential peptidoglycan cleavage in Mycobacterium tuberculosis during infection [MtrA_OE_pH]

2021-07-16 | GSE166804 | GEO

Identification of a new family of peptidoglycan transpeptidases reveals unusualcrosslinking is essential for viability inC. difficile

Project description:Most bacteria are surrounded by a peptidoglycan cell wall composed of glycan strands held together by short peptide crosslinks. There are two major types of crosslinks, termed 4-3 and 3-3 based on the amino acids involved. 4-3 crosslinks are created by penicillin-binding proteins (PBPs), while 3-3 crosslinks created byL,D-transpeptidases (LDTs). In well studied bacteria 3-3 crosslinks comprise only about 10% of the total and are not essential. However, in the opportunistic intestinal pathogenClostridioides difficile,about 70% of the crosslinks are 3-3. We show here that 3-3 crosslinks and LDTs are essential for viability inC. difficile. We also show thatC. difficilehas five LDTs, three with a YkuD catalytic domain as in all previously known LDTs and two with a VanW catalytic domain, whose function was until now unknown. The five LDTs exhibit extensive functional redundancy. VanW domain proteins are found in many Gram-positive bacteria but scarce in other lineages. We tested seven non-C. difficileVanW domain proteins and confirmed LDT activity in three cases. In summary, our findings uncover a new family of peptidoglycan crosslinking enzymes, assign a catalytic function to VanW domains, and demonstrate that 3-3 crosslinking is essential for viability inC. difficile, the first time this has been shown in any bacterial species.

2024-07-30 | GSE270128 | GEO

Expression data from peptidoglycan stimulated CD11b+ cells from NOD and NOD.Idd3

Project description:CD11b+ CD11c- cells were isolated by cell sorting from the spleens of NOD and NOD.Idd3 mice. Cells were then either unstimulated or stimulated with peptidoglycan (5ug/ml) for 4 hours at 37 degrees prior to RNA extraction. Peptidoglycan was chosen as a stimulus due to its know ability to stimulate CD11b+ cells through Toll-like receptor 2 and our previous data showing biological differences between NOD and NOD.Idd3-derived CD11b+CD11c- cells after stimulation with peptidoglycan. CD11b+ cells from NOD and NOD.Idd3 were either unstimulated or stimulated with peptidoglycan(PGN) for 4 hours at 37 degerees prior to RNA extraction.

2010-09-28 | E-GEOD-24350 | biostudies-arrayexpress

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