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The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis.

ABSTRACT: The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis.

PROVIDER: PRJNA797998 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17642980_1.fastq.gz	Fastqsanger.gz
	SRR17642980_2.fastq.gz	Fastqsanger.gz
	SRR17642981_1.fastq.gz	Fastqsanger.gz
	SRR17642981_2.fastq.gz	Fastqsanger.gz
	SRR17642982_1.fastq.gz	Fastqsanger.gz

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The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis. [ChIP-Seq]

Project description:Although two Enhancer of Polycomb-like proteins, EPL1A and EPL1B (EPL1A/B), are known to be conserved and characteristic subunits of the NuA4-type histone acetyltransferase complex in Arabidopsis thaliana, the biological function of EPL1A/B and the mechanism by which EPL1A/B function in the complex remain unknown. Here, we report that EPL1A/B are required for the histone acetyltransferase activity of the NuA4 complex on the nucleosomal histone H4 in vitro and for the enrichment of histone H4K5 acetylation at thousands of protein-coding genes in vivo. We demonstrate that EPL1A/B are required for linking the NuA4 catalytic subunit HAM1 with accessory subunits in the NuA4 complex. EPL1A/B function redundantly in regulating plant development especially in chlorophyll biosynthesis and de-etiolation. The EPL1A/B-dependent transcription and H4K5Ac are enriched at genes involved in chlorophyll biosynthesis and photosynthesis. We also find that EAF6, another characteristic subunit of the NuA4 complex, contribute to de-etiolation. These results suggest that the Arabidopsis NuA4 complex components function as a whole to mediate histone acetylation and transcriptional activation specifically at light-responsive genes and are critical for photomorphogenesis.

2022-01-20 | GSE193793 | GEO

The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis. [RNA-Seq]

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The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis. [RNA-Seq]

Project description:The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis. [RNA-Seq]

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The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis. [ChIP-Seq]

Project description:The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis. [ChIP-Seq]

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The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis.

Project description:This SuperSeries is composed of the SubSeries listed below.

2022-01-20 | GSE193794 | GEO

An epitranscriptomic mechanism regulating chlorophyll biosynthesis in Arabidopsis

Project description:Light modulates expression of nuclear-encoded chloroplast proteins to promote chlorophyll biosynthesis and photosynthesis in plants. Photoregulatory mechanisms regulating transcription and protein stability of nuclear-encoded chloroplast proteins have been extensively studied, but how photoresponsive mRNA metabolism affecting chloroplast proteins remains not well understood. We performed a systematic analysis of the photoresponsive transcriptomes, m6A epitranscriptomes, translatomes, and proteomes in Arabidopsis, leading to a hypothesis that the blue light receptor cryptochromes activate the RNA methyltransferase, FIONA 1 (FIO1), to increase RNA methylation, translation of the nuclear-encoded chlorophyll synthesis enzymes (CSEs), and chlorophyll synthesis. We further demonstrate that the photoresponsive CRY2-interacting protein, SPA1, acts as a chaperone to mediate co-condensation of the CRY2/FIO1 complex, activating the FIO1 methyltransferase activity. This finding demonstrates a previously unknown photoregulatory mechanism controlling chlorophyll biosynthesis in plants.

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Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex [RNA-seq]

Project description:The human NuA4/TIP60 co-activator complex, a fusion of the yeast SWR1 and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4/H2A/H2A.Z to play crucial roles regulating gene expression and maintaining genome stability. Our cryo-EM studies show that within the NuA4/TIP60 complex, the EP400 subunit serves as an architectural scaffold holding the different functional modules in specific positions and giving rise to a novel arrangement of the ARP module. EP400 interacts with the TRRAP subunit using a footprint that overlaps with that of the SAGA acetyltransferase complex, thereby preventing the formation of a hybrid complex. Loss of the TRRAP subunit leads to mislocalization of NuA4/TIP60, resulting in the redistribution of H2A.Z and its acetylation across the genome, emphasizing the dual functionality of NuA4/TIP60 as a single macromolecular assembly.

2024-08-06 | GSE261651 | GEO

Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex [ChIP-seq]

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Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex

2024-08-08 | PXD053209 | Pride

Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex

Project description:The human NuA4/TIP60 co-activator complex, a fusion of the yeast SWR1 and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4/H2A/H2A.Z to play crucial roles regulating gene expression and maintaining genome stability. Our cryo-EM studies show that within the NuA4/TIP60 complex, the EP400 subunit serves as an architectural scaffold holding the different functional modules in specific positions and giving rise to a novel arrangement of the ARP module. EP400 interacts with the TRRAP subunit using a footprint that overlaps with that of the SAGA acetyltransferase complex, thereby preventing the formation of a hybrid complex. Loss of the TRRAP subunit leads to mislocalization of NuA4/TIP60, resulting in the redistribution of H2A.Z and its acetylation across the genome,emphasizing the dual functionality of NuA4/TIP60 as a single macromolecular assembly.

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