Evidence map›Paper›PMID 27151214›Full record

ArticleThe Journal of biological chemistry2016

Insights into the Unique Phosphorylation of the Lasso Peptide Paeninodin.

Shaozhou Zhu, Julian D Hegemann, Christopher D Fage, Marcel Zimmermann, Xiulan Xie, Uwe Linne, Mohamed A Marahiel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
7.7field-weighted citation impact, top 2% of its field
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

95 citing papers in PubMed, 160 citations in OpenAlex.

  1. Article
  2. Article
  3. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  4. Draft genome sequence of epiphyteMicrobiology resource announcements · 2026
    Article
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Proposal ofInternational journal of molecular sciences · 2025
    Article
  14. Microbiology resource announcements · 2025
    Article
  15. Lasso Peptides-A New Weapon Against Superbugs.International journal of molecular sciences · 2025
    Review
  16. Article
  17. Applied and environmental microbiology · 2025
    Article
  18. Evolution-Guided Discovery of Antimycobacterial Triculamin-Like Lasso Peptides.Angewandte Chemie (International ed. in English) · 2025
    Article
  19. Article
  20. Article

35 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

7 authors at 2 institutions in 1 country.

Shaozhou ZhuFrom the Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, 35032 Marburg, Germany.
Julian D HegemannFrom the Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, 35032 Marburg, Germany.
Christopher D FageFrom the Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, 35032 Marburg, Germany.
Marcel ZimmermannFrom the Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, 35032 Marburg, Germany.
Xiulan XieFrom the Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, 35032 Marburg, Germany.
Uwe LinneFrom the Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, 35032 Marburg, Germany.
Mohamed A MarahielFrom the Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, 35032 Marburg, Germany marahiel@staff.uni-marburg.de.
Philipps University of Marburg · DELoewe Center for Synthetic Microbiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lasso peptides are a new class of ribosomally synthesized and post-translationally modified peptides and thus far are only isolated from proteo- and actinobacterial sources. Typically, lasso peptide biosynthetic gene clusters encode enzymes for biosynthesis and export but not for tailoring. Here, we describe the isolation of the novel lasso peptide paeninodin from the firmicute Paenibacillus dendritiformis C454 and reveal within its biosynthetic cluster a gene encoding a kinase, which we have characterized as a member of a new class of lasso peptide-tailoring kinases. By employing a wide variety of peptide substrates, it was shown that this novel type of kinase specifically phosphorylates the C-terminal serine residue while ignoring those located elsewhere. These experiments also reveal that no other recognition motif is needed for efficient enzymatic phosphorylation of the C-terminal serine. Furthermore, through comparison with homologous HPr kinases and subsequent mutational analysis, we confirmed the essential catalytic residues. Our study reveals how lasso peptides are chemically diversified and sets the foundation for rational engineering of these intriguing natural products.

Indexed as

Bacterial ProteinsPaenibacillusPeptidesPhosphorylationProtein Processing, Post-TranslationalBacterial ProteinsPeptidesBacillusbiosynthesisFirmicuteskinaseLasso peptidenatural productphosphorylationpost-translational modificationRiPP

Identifiers

PMID27151214
PMCPMC4919450
OpenAlexW2346922803

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.