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Characterization of the RNA present in L1 ORF1p macromolecular complexes from Mael-/- mouse testes

ABSTRACT: Characterization of the RNA present in L1 ORF1p macromolecular complexes from Mael-/- mouse testes

PROVIDER: PRJNA922048 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR23021829.fastq.gz	Fastqsanger.gz
	SRR23021830.fastq.gz	Fastqsanger.gz
	SRR23021831.fastq.gz	Fastqsanger.gz
	SRR23021832.fastq.gz	Fastqsanger.gz
	SRR23021833.fastq.gz	Fastqsanger.gz

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Characterization of the RNA present in L1 ORF1p macromolecular complexes from Mael-/- mouse testes

Project description:piRNA-deficient Maelstrom (Mael) null mice are characterized by a strong upregulation of LINE-1 (L1) retrotransposon in meiotic spermatocytes. This defect turns out in the accumulation of L1 RNA and ORF1p in their cytoplasm and the formation of prominent ribonucleoprotein aggregates. We used 3-months-old Mael-/- male mice to characterize the RNA present in those ORF1p aggregates. To favor the isolation of complexed versus free ORF1p protein, we first fractionated Mael-/- testis extracts (that we refer to as TOTAL) by sucrose gradient ultracentrifugation, in the presence of EDTA. We then pooled the sucrose fractions where ORF1p macromolecular complexes sediment (fractions 5-8) and used this pool as the INPUT for an anti-ORF1p co-immunoprecipitation (IP) followed by RNA-seq.

2023-05-25 | GSE222416 | GEO

Characterization of L1 ORF1p macromolecular complexes from Mael-/- mouse testes

Project description:piRNA-deficient Maelstrom (Mael) null mice are characterized by a strong upregulation of retrotransposon LINE-1 (L1) in meiotic spermatocytes. This defect turns out in the accumulation of L1 RNA and ORF1p in their cytoplasm and the formation of prominent ribonucleoprotein aggregates. We used 3-months-old Mael-/- male mice to characterize the protein composition of those ORF1p aggregates.

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Project description:Long Interspersed Nuclear Element-1 (LINE-1, L1) is a mobile genetic element active in human genomes. L1-encoded ORF1 and ORF2 proteins bind L1 RNAs, forming ribonucleoproteins (RNPs). These RNPs interact with diverse host proteins, some repressive and others required for the L1 lifecycle. Using differential affinity purifications, quantitative mass spectrometry, and next generation RNA sequencing, we have characterized the proteins and nucleic acids associated with distinctive, enzymatically active L1 macromolecular complexes. Among them, we describe a cytoplasmic intermediate that we hypothesize to be the canonical ORF1p/ORF2p/L1-RNA-containing RNP, and we describe a nuclear population containing ORF2p, but lacking ORF1p, which likely contains host factors participating in target-primed reverse transcription.

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