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A Phase-Separated Nuclear GBPL Circuit Controls Immunity in Plants

ABSTRACT: A Phase-Separated Nuclear GBPL Circuit Controls Immunity in Plants

PROVIDER: PRJNA556000 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR9729450_1.fastq.gz	Fastqsanger.gz
	SRR9729450_2.fastq.gz	Fastqsanger.gz
	SRR9729451_1.fastq.gz	Fastqsanger.gz
	SRR9729451_2.fastq.gz	Fastqsanger.gz
	SRR9729452_1.fastq.gz	Fastqsanger.gz

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A Phase-Separated Nuclear GBPL Circuit Controls Immunity in Plants

Project description:Liquid-liquid phase separation (LLPS) has emerged as a central paradigm for understanding how membrane-less organelles compartmentalize diverse cellular activities in eukaryotes. Here, we identified a new superfamily of plant Guanylate Binding Protein-Like GTPases (GBPLs) that assemble LLPS-driven condensates within the nucleus to protect against infection and autoimmunity. In Arabidopsis thaliana, two family members - GBPL1 and GBPL3 - undergo phase transition behavior to control transcriptional responses as part of an allosteric switch triggered by exposure to biotic stress. GBPL1, a pseudoGTPase, sequesters catalytically-active GBPL3 under basal conditions but is displaced by LLPS when GBPL3 enters the nucleus following immune cues to drive formation of unique membrane-less organelles termed GDACs (GBPL Defense-Activated Condensates) that we visualized by in situ cryo-electron tomography. Within these mesoscale GDAC structures, native GBPL3 directly bound defense gene promoters and recruited specific transcriptional coactivators of the Mediator complex plus RNA Pol II machinery to massively reprogram host gene expression for disease resistance. Together, our study identifies a new GBPL circuit that reinforces the biological importance of phase-separated condensates, in this case, as indispensable players in plant defense.

2021-03-24 | GSE134651 | GEO

A phase-separated nuclear GBPL circuit controls immunity in plants.

Project description:Liquid-liquid phase separation (LLPS) has emerged as a central paradigm for understanding how membraneless organelles compartmentalize diverse cellular activities in eukaryotes1-3. Here we identify a superfamily of plant guanylate-binding protein (GBP)-like GTPases (GBPLs) that assemble LLPS-driven condensates within the nucleus to protect against infection and autoimmunity. In Arabidopsis thaliana, two members of this family-GBPL1 and GBPL3-undergo phase-transition behaviour to control transcriptional responses as part of an allosteric switch that is triggered by exposure to biotic stress. GBPL1, a pseudo-GTPase, sequesters catalytically active GBPL3 under basal conditions but is displaced by GBPL3 LLPS when it enters the nucleus following immune cues to drive the formation of unique membraneless organelles termed GBPL defence-activated condensates (GDACs) that we visualized by in situ cryo-electron tomography. Within these mesoscale GDAC structures, native GBPL3 directly bound defence-gene promoters and recruited specific transcriptional coactivators of the Mediator complex and RNA polymerase II machinery to massively reprogram host gene expression for disease resistance. Together, our study identifies a GBPL circuit that reinforces the biological importance of phase-separated condensates, in this case, as indispensable players in plant defence.

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Stress response by phase-separated p62

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Phase-separated CCER1 coordinates histone-to-protamine transition and fertility

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lncRNA DIGIT and BRD3 protein form phase-separated condensates to regulate endoderm differentiation [RIP-seq]

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Project description:HIV-1 latency is a major obstacle to achieve a functional cure for AIDS. To eradicate the viral reservoir, one of the strategies is to specifically reactivate HIV-1-infected cells and followed by elimination with potent immune surveillance. However, present latency-reversing agents (LRAs) are quite dissatisfactory because of their high toxicity and low efficiency. New targets need to be identified to develop more promising LRAs. Here, we found that histone chaperone chromatin assembly factor 1 (CAF-1) promotes HIV-1 latency by forming versatile suppressive nuclear bodies. CAF-1 plays a leading role for the formation of bodies recruiting multi-layer suppressive epigenetic modifiers and maintainers, and is of the characteristic of liquid-liquid phase separation (LLPS). Three distinct disordered regions of CHAF1A subunit coalesce CAF-1 body components by forming LLPS and play a key in maintaining HIV-1 latency. Therefore, disruptive induction of phase-separated CAF-1 body could be an important strategy to reactivate latent HIV-1.

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Phase-separated CCER1 coordinates histone-to-protamine transition and fertility

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