Evidence map›Paper›PMID 25402768›Full record

ArticleNature chemical biology2015

A peptide ligase and the ribosome cooperate to synthesize the peptide pheganomycin.

Motoyoshi Noike, Takashi Matsui, Koichi Ooya, Ikuo Sasaki, Shouta Ohtaki, Yoshimitsu Hamano, Chitose Maruyama, Jun Ishikawa, Yasuharu Satoh, Hajime Ito and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Cytochromes P450 involved in bacterial RiPP biosyntheses.Journal of industrial microbiology & biotechnology · 2023
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Enzymkatalysierte späte Modifizierungen: Besser spät als nie.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Review
  14. Enzymatic Late-Stage Modifications: Better Late Than Never.Angewandte Chemie (International ed. in English) · 2021
    Review
  15. Article
  16. Article
  17. AApplied and environmental microbiology · 2021
    Article
  18. Review
  19. Article
  20. Article
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

12 authors at 4 institutions in 1 country.

Motoyoshi NoikeGraduate School of Engineering, Hokkaido University, Hokkaido, Japan.
Takashi MatsuiInstitute of Natural Medicine, University of Toyama, Toyama, Japan.
Koichi OoyaGraduate School of Engineering, Hokkaido University, Hokkaido, Japan.
Ikuo SasakiGraduate School of Engineering, Hokkaido University, Hokkaido, Japan.
Shouta OhtakiInstitute of Natural Medicine, University of Toyama, Toyama, Japan.
Yoshimitsu HamanoDepartment of Bioscience, Fukui Prefectural University, Fukui, Japan.
Chitose MaruyamaDepartment of Bioscience, Fukui Prefectural University, Fukui, Japan.
Jun IshikawaNational Institute of Infectious Diseases, Tokyo, Japan.
Yasuharu SatohGraduate School of Engineering, Hokkaido University, Hokkaido, Japan.
Hajime ItoGraduate School of Engineering, Hokkaido University, Hokkaido, Japan.
Hiroyuki MoritaInstitute of Natural Medicine, University of Toyama, Toyama, Japan.
Tohru DairiGraduate School of Engineering, Hokkaido University, Hokkaido, Japan.
Hokkaido University · JPUniversity of Toyama · JPFukui Prefectural University · JPNational Institute of Infectious Diseases · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptide antibiotics are typically biosynthesized by one of two distinct machineries in a ribosome-dependent or ribosome-independent manner. Pheganomycin (PGM (1)) and related analogs consist of the nonproteinogenic amino acid (S)-2-(3,5-dihydroxy-4-hydroxymethyl)phenyl-2-guanidinoacetic acid (2) and a proteinogenic core peptide, making their origin uncertain. We report the identification of the biosynthetic gene cluster from Streptomyces cirratus responsible for PGM production. Unexpectedly, the cluster contains a gene encoding multiple precursor peptides along with several genes plausibly encoding enzymes for the synthesis of amino acid 2. We identified PGM1, which has an ATP-grasp domain, as potentially capable of linking the precursor peptides with 2, and validate this hypothesis using deletion mutants and in vitro reconstitution. We document PGM1's substrate permissivity, which could be rationalized by a large binding pocket as confirmed via structural and mutagenesis experiments. This is to our knowledge the first example of cooperative peptide synthesis achieved by ribosomes and peptide ligases using a peptide nucleophile.

Indexed as

Anti-Bacterial AgentsLigasesModels, MolecularMolecular Sequence DataMultigene FamilyMutagenesisPeptidesProtein ConformationRibosomesStreptomycesAnti-Bacterial AgentsLigasesPeptidespheganomycin

Identifiers

PMID25402768
OpenAlexW2023397345

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.