ArticleNature communications2017
Single-peptide DNA-dependent RNA polymerase homologous to multi-subunit RNA polymerase.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Exosomes delivering a high-throughput-screened RNA polymerase inhibitor for highly effective therapy of multidrug-resistant bacterial infected pneumonia.Bioactive materials · 2026Article
- DragonRNA: Generality of DNA-primed RNA-extension activities by DNA-directed RNA polymerases.Nucleic acids research · 2025Article
- iModulonMiner and PyModulon: Software for unsupervised mining of gene expression compendia.PLoS computational biology · 2024Article
- Tail-tape-fused virion and non-virion RNA polymerases of a thermophilic virus with an extremely long tail.Nature communications · 2024Article
- synphage: a pipeline for phage genome synteny graphics focused on gene conservation.Bioinformatics advances · 2024Article
- Reclassification of family A DNA polymerases reveals novel functional subfamilies and distinctive structural features.Nucleic acids research · 2023Article
- Dormant phages communicate via arbitrium to control exit from lysogeny.Nature microbiology · 2022Article
- The life cycle of SPβ and related phages.Archives of virology · 2021Review
- Widespread divergent transcription from bacterial and archaeal promoters is a consequence of DNA-sequence symmetry.Nature microbiology · 2021Article
- Multisubunit RNA Polymerases of Jumbo Bacteriophages.Viruses · 2020Review
- A distinct lineage of Caudovirales that encodes a deeply branching multi-subunit RNA polymerase.Nature communications · 2020Article
- Molecular crowding induces primer extension by RNA polymerase through base stacking beyond Watson-Crick rules.RSC advances · 2020Article
- High intrinsic hydrolytic activity of cyanobacterial RNA polymerase compensates for the absence of transcription proofreading factors.Nucleic acids research · 2020Article
- Enhanced Expression of Pullulanase inFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Transcription in all living organisms is accomplished by multi-subunit RNA polymerases (msRNAPs). msRNAPs are highly conserved in evolution and invariably share a ∼400 kDa five-subunit catalytic core. Here we characterize a hypothetical ∼100 kDa single-chain protein, YonO, encoded by the SPβ prophage of Bacillus subtilis. YonO shares very distant homology with msRNAPs, but no homology with single-subunit polymerases. We show that despite homology to only a few amino acids of msRNAP, and the absence of most of the conserved domains, YonO is a highly processive DNA-dependent RNA polymerase. We demonstrate that YonO is a bona fide RNAP of the SPβ bacteriophage that specifically transcribes its late genes, and thus represents a novel type of bacteriophage RNAPs. YonO and related proteins present in various bacteria and bacteriophages have diverged from msRNAPs before the Last Universal Common Ancestor, and, thus, may resemble the single-subunit ancestor of all msRNAPs.
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