Evidence map›Paper›PMID 30916321›Full record

ArticleNucleic acids research2019

Uncovering the unexplored diversity of thioamidated ribosomal peptides in Actinobacteria using the RiPPER genome mining tool.

Javier Santos-Aberturas, Govind Chandra, Luca Frattaruolo, Rodney Lacret, Thu H Pham, Natalia M Vior, Tom H Eyles, Andrew W Truman

Abstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

84 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Heme oxygenase-like dimetal oxidases and oxygenases.Biochemical Society transactions · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Heme Oxygenase-Like Metalloenzymes.Annual review of biochemistry · 2025
    Review
  16. Evolution-Guided Discovery of Antimycobacterial Triculamin-Like Lasso Peptides.Angewandte Chemie (International ed. in English) · 2025
    Article
  17. Article
  18. Review
  19. Article
  20. Review

24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Javier Santos-AberturasDepartment of Molecular Microbiology, John Innes Centre, Norwich, Norfolk NR4 7UH, UK.
Govind ChandraDepartment of Molecular Microbiology, John Innes Centre, Norwich, Norfolk NR4 7UH, UK.
Luca FrattaruoloDepartment of Molecular Microbiology, John Innes Centre, Norwich, Norfolk NR4 7UH, UK.
Rodney LacretDepartment of Molecular Microbiology, John Innes Centre, Norwich, Norfolk NR4 7UH, UK.
Thu H PhamDepartment of Molecular Microbiology, John Innes Centre, Norwich, Norfolk NR4 7UH, UK.
Natalia M ViorDepartment of Molecular Microbiology, John Innes Centre, Norwich, Norfolk NR4 7UH, UK.
Tom H EylesDepartment of Molecular Microbiology, John Innes Centre, Norwich, Norfolk NR4 7UH, UK.
Andrew W TrumanDepartment of Molecular Microbiology, John Innes Centre, Norwich, Norfolk NR4 7UH, UK.

Funding

Biotechnology and Biological Sciences Research Council BBS/E/J/000PR9790
6 · The paper itself

Abstract

The rational discovery of new specialized metabolites by genome mining represents a very promising strategy in the quest for new bioactive molecules. Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a major class of natural product that derive from genetically encoded precursor peptides. However, RiPP gene clusters are particularly refractory to reliable bioinformatic predictions due to the absence of a common biosynthetic feature across all pathways. Here, we describe RiPPER, a new tool for the family-independent identification of RiPP precursor peptides and apply this methodology to search for novel thioamidated RiPPs in Actinobacteria. Until now, thioamidation was believed to be a rare post-translational modification, which is catalyzed by a pair of proteins (YcaO and TfuA) in Archaea. In Actinobacteria, the thioviridamide-like molecules are a family of cytotoxic RiPPs that feature multiple thioamides, which are proposed to be introduced by YcaO-TfuA proteins. Using RiPPER, we show that previously undescribed RiPP gene clusters encoding YcaO and TfuA proteins are widespread in Actinobacteria and encode a highly diverse landscape of precursor peptides that are predicted to make thioamidated RiPPs. To illustrate this strategy, we describe the first rational discovery of a new structural class of thioamidated natural products, the thiovarsolins from Streptomyces varsoviensis.

Indexed as

ActinobacteriaBiological ProductsDNA-Directed DNA PolymeraseGenomePeptide BiosynthesisPeptidesPeptides, CyclicProtein Processing, Post-TranslationalRibosomesStreptomycesThioamidesBiological ProductsDNA-Directed DNA PolymeraseDNA polymerase TfuPeptidesPeptides, CyclicThioamidesthioviridamide

Identifiers

PMID30916321
PMCPMC6511847

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.