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An siRNA-guided AGO protein recruits Polymerase V to initiate RNA-directed DNA methylation

ABSTRACT: An siRNA-guided AGO protein recruits Polymerase V to initiate RNA-directed DNA methylation

PROVIDER: PRJNA694981 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR13537400.fastq.gz	Fastqsanger.gz
	SRR13537401.fastq.gz	Fastqsanger.gz
	SRR13537402.fastq.gz	Fastqsanger.gz
	SRR13537403.fastq.gz	Fastqsanger.gz
	SRR13537404.fastq.gz	Fastqsanger.gz

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An siRNA-guided AGO protein recruits Polymerase V to initiate RNA-directed DNA methylation (BSA-seq dataset)

Project description:An siRNA-guided AGO protein recruits Polymerase V to initiate RNA-directed DNA methylation (BSA-seq dataset)

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An siRNA-guided AGO protein recruits Polymerase V to initiate RNA-directed DNA methylation (smallRNA-seq dataset)

Project description:Foreign DNA is silenced in plants by small RNA-directed DNA methylation (RdDM). RNA Polymerase V (Pol V) is the key protein required to recruit DNA methyltransferases to a RdDM target region. However, the mechanism required for the initial recruitment of Pol V to a targeted locus remains a mystery. In this study, we used first generation (T1) transgene transformations to elucidate a novel mechanism by which Pol V is recruited to both new transgenic and endogenous loci. This study is heavily dependent on analyzing the DNA methylation pattern and small RNAs produced from specific loci. All small RNA sequences (sRNA-seq) and bisulfite converted amplicon sequencing data (BSAS) used in this study are submitted as part of this data series.

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Project description:During microRNA (miRNA)-guided gene silencing, Argonaute (Ago) proteins interact with a member of the TNRC6/GW protein family. Here we used a short GW protein-derived peptide fused to GST and demonstrate that it binds to Ago proteins with high affinity. This allows for the simultaneous isolation of all Ago protein complexes expressed in diverse species to identify associated proteins, small RNAs or target mRNAs. We refer to our method as Ago protein Affinity Purification by Peptides (Ago-APP). Comparison of small RNA lengths in total RNA and APP-enriched RNA samples

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AGO pathway

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Maternal inherited siRNA initiate piRNA cluster formation

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Redundant AGO-hook platforms and AGO4-DNA interaction in polV-directed RdDM

Project description:Small RNA-dependent pairing of AGO/PIWI-containing effector complexes to chromatin-bound nascent transcripts has been proposed as a universal mechanism for guiding RNA-mediated TGS in eukaryotes. Likewise, Pol V-dependent transcripts have been implicated in the targeting of AGO4 to chromatin in RNA-directed DNA methylation (RdDM) in plants. Here, we show that the AGO hook platforms of PolV and SPT5L, another component of the transcriptional complex, are functionally redundant yet essential for RdDM at a genome-wide level. Synthesis of Pol V transcripts is uncoupled from AGO4 recruitment in AGO hook-minus plants, challenging the prevailing RNA-based mechanism of AGO4 targeting to chromatin in RdDM. Transcription is essential to lock the PolV transcription complex into a stable and productive DNA-bound state potentiating interactions of AGO4 with DNA. Consistent with this idea, laser UV-assisted crosslinking shows specific AGO4-DNA interaction at RdDM loci, suggesting a revised model for Pol V-mediated DNA methylation in plants, which explains the exquisite specificity of methylation.

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