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P23 acts as an RNA binding protein, which interacts differentially with specific mRNAs in response to LPS and modulates the macrophage inflammation response

ABSTRACT: P23 acts as an RNA binding protein, which interacts differentially with specific mRNAs in response to LPS and modulates the macrophage inflammation response

PROVIDER: PRJNA669843 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12842414_1.fastq.gz	Fastqsanger.gz
	SRR12842414_2.fastq.gz	Fastqsanger.gz
	SRR12842415_1.fastq.gz	Fastqsanger.gz
	SRR12842415_2.fastq.gz	Fastqsanger.gz
	SRR12842416_1.fastq.gz	Fastqsanger.gz

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P23 acts as an RNA binding protein, which interacts differentially with specific mRNAs in response to LPS and modulates the macrophage inflammation response

Project description:We report the identification of RNAs bound by P23, which was previously uncovered as new poly(A+)-RNA interacting protein in murine RAW 264.7 macrophages (Liepelt, et al., 2016). RNAseq of RNAs immunoprecipitated with P23 revealed that specifc mRNAs were bound differentially in untreated and in LPS-activated RAW 264.7 cells.

2021-06-09 | GSE159619 | GEO

Chromatin immunoprecipitation DNA-sequencing (ChIP-seq) for RNA-polymerases encoded by P23-45 bacteriophage

Project description:By doing ChIP-seq with antibodies against two P23-45 RNA polymerases gp64 and gp96 we showed that both RNA polymerases interact with the phage genome at the early stage of infection. Gp96 interacts with pre-early P23-45 genes, while gp64 interacts with pre-early, early and some middle-stage genes.

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Pseudomonas aeruginosa strain:P23 | isolate:P23

Project description:Pseudomonas aeruginosa strain:P23 | isolate:P23 Genome sequencing

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P23 Acts as Functional RBP in the Macrophage Inflammation Response.

Project description:Macrophages exert the primary cellular immune response. Pathogen components like bacterial lipopolysaccharides (LPS) stimulate macrophage migration, phagocytotic activity and cytokine expression. Previously, we identified the poly(A)+ RNA interactome of RAW 264.7 macrophages. Of the 402 RNA-binding proteins (RBPs), 32 were classified as unique in macrophages, including nineteen not reported to interact with nucleic acids before. Remarkably, P23 a HSP90 co-chaperone, also known as cytosolic prostaglandin E2 synthase (PTGES3), exhibited differential poly(A)+ RNA binding in untreated and LPS-induced macrophages. To identify mRNAs bound by P23 and to elucidate potential regulatory RBP functions in macrophages, we immunoprecipitated P23 from cytoplasmic extracts of cross-linked untreated and LPS-induced cells. RNAseq revealed that enrichment of 44 mRNAs was reduced in response to LPS. Kif15 mRNA, which encodes kinesin family member 15 (KIF15), a motor protein implicated in cytoskeletal reorganization and cell mobility was selected for further analysis. Noteworthy, phagocytic activity of LPS-induced macrophages was enhanced by P23 depletion. Specifically, in untreated RAW 264.7 macrophages, decreased P23 results in Kif15 mRNA destabilization, diminished KIF15 expression and accelerated macrophage migration. We show that the unexpected RBP function of P23 contributes to the regulation of macrophage phagocytotic activity and migration.

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A direct interplay between the co-chaperones Hop and p23 regulates cycle progression and client folding in the Hsp70/Hsp90 chaperone machineries

Project description:Folding of stringent clients requires transfer from Hsp70 to Hsp90. The co-chaperone Hop physically connects the chaperone machineries. Here we define its role from the remodeling of Hsp70/40-client complexes to the mechanism of client transfer and the conformational switching from stalled to active client-processing states of Hsp90. We show that Hsp70 together with Hsp40 completely unfolds a stringent client, the glucocorticoid receptor ligand binding domain (GR-LBD) in large assemblies. Hop remodels these for efficient transfer onto Hsp90. As p23 enters, Hsp70 leaves the complex via switching between binding sites in Hop. To proceed to client folding, current concepts assume that Hop dissociates and the co-chaperone p23 stabilizes the Hsp90 closed state. In contrast, we show that p23 directly interacts with Hop, relieves the stalling Hsp90-Hop interaction and closes Hsp90. This reaction allows folding of the client and is thus the key regulatory step for the progression of the chaperone cycle. To study the interaction between the different proteins, especially p23 and the DP2 domain of Hop, we performed crosslinking-MS.

2022-02-24 | PXD027413 | Pride

Vibrio phage P23

Project description:Vibrio phage P23 Genome sequencing and assembly

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Clostridioides difficile P23

Project description:Clostridioides difficile P23 Genome sequencing and assembly

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Acinetobacter calcoaceticus strain:P23

Project description:Acinetobacter calcoaceticus P23 genome sequencing project

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Phaeobacter piscinae strain:P23

Project description:Phaeobacter piscinae strain:P23 Genome sequencing