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Protein-primed DNA homopolymer synthesis by an antiviral reverse transcriptase [cDIP-seq]

ABSTRACT: Protein-primed DNA homopolymer synthesis by an antiviral reverse transcriptase [cDIP-seq]

PROVIDER: PRJNA1256746 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR33366700_1.fastq.gz	Fastqsanger.gz
	SRR33366700_2.fastq.gz	Fastqsanger.gz
	SRR33366701_1.fastq.gz	Fastqsanger.gz
	SRR33366701_2.fastq.gz	Fastqsanger.gz
	SRR33366702_1.fastq.gz	Fastqsanger.gz

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Protein-primed DNA homopolymer synthesis by an antiviral reverse transcriptase [RNA-seq]

Project description:Protein-primed DNA homopolymer synthesis by an antiviral reverse transcriptase [RNA-seq]

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Protein-primed DNA homopolymer synthesis by an antiviral reverse transcriptase [RNA-seq]

Project description:Bacteria defend themselves from viral predation using diverse immune systems, many of which sense and target foreign DNA for degradation. Defense-associated reverse transcriptase (DRT) systems provide an intriguing counterpoint to this strategy by leveraging DNA synthesis instead. We and others recently showed that DRT2 systems use an RNA template to assemble a de novo gene, leading to expression of an antiviral effector protein, Neo. It remains unknown whether similar mechanisms of defense are employed by other related DRT families. Focusing on DRT9, here we uncover an unprecedented mechanism of DNA homopolymer synthesis, in which viral infection triggers polydeoxyadenylate (poly-dA) accumulation in the cell to drive abortive infection and population-level immunity. Cryo-EM structures reveal how a conserved noncoding RNA serves as both a structural scaffold and reverse transcription template to direct hexameric complex assembly and RNA-templated poly-dA synthesis. Remarkably, biochemical and functional experiments identify conserved tyrosine residues within the reverse transcriptase itself that prime DNA synthesis, leading to the formation of high-molecular weight protein-DNA covalent adducts. Synthesis of poly-dA in vivo is regulated by the competing activities of phage-encoded triggers and host-encoded silencers of DRT9. Collectively, our work unveils a novel nucleic acid-driven defense system that expands the paradigm of bacterial immunity and broadens the known functions of reverse transcriptases.

2025-05-09 | GSE295897 | GEO

Protein-primed DNA homopolymer synthesis by an antiviral reverse transcriptase [RIP-seq]

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2025-05-09 | GSE295895 | GEO

De novo gene synthesis by an antiviral reverse transcriptase

Project description:De novo gene synthesis by an antiviral reverse transcriptase

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De novo gene synthesis by an antiviral reverse transcriptase [cDIP-seq]

Project description:De novo gene synthesis by an antiviral reverse transcriptase [cDIP-seq]

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De novo gene synthesis by an antiviral reverse transcriptase [RIP-seq]

Project description:De novo gene synthesis by an antiviral reverse transcriptase [RIP-seq]

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De novo gene synthesis by an antiviral reverse transcriptase [RNA-seq]

Project description:De novo gene synthesis by an antiviral reverse transcriptase [RNA-seq]

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De novo gene synthesis by an antiviral reverse transcriptase [RNA-seq]

Project description:Bacteria defend themselves from viral predation using diverse immune systems, many of which sense and target foreign nucleic acids. Defense-associated reverse transcriptase (DRT) systems provide an intriguing counterpoint to this immune strategy by instead leveraging DNA synthesis, but the identities and functions of their DNA products remain largely unknown. Here we show that DRT2 systems execute an unprecedented immunity mechanism that involves de novo gene synthesis via rolling-circle reverse transcription of a non-coding RNA (ncRNA). Unbiased profiling of RT-associated RNA and DNA ligands uncovered constitutive synthesis of concatenated cDNA repeats through programmed template jumping on the ncRNA. The presence of phage then triggers second-strand cDNA synthesis, leading to the production of long double-stranded DNA. Remarkably, this nascent ‘gene’ is efficiently transcribed, generating messenger RNAs that encode a stop codon-less, never-ending ORF (neo) whose translation causes potent growth arrest. Phylogenetic analyses and screening of diverse DRT2 homologs further revealed broad conservation of rolling-circle reverse transcription and Neo protein function. Our work highlights an elegant expansion of genome coding potential through RNA-templated gene creation, and challenges conventional paradigms of genetic information encoded along the one-dimensional axis of genomic DNA.

2024-08-11 | GSE270162 | GEO

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