Evidence map›Paper›PMID 29039940›Full record

ArticleJournal of the American Chemical Society2017

NosN, a Radical S-Adenosylmethionine Methylase, Catalyzes Both C1 Transfer and Formation of the Ester Linkage of the Side-Ring System during the Biosynthesis of Nosiheptide.

Joseph W LaMattina, Bo Wang, Edward D Badding, Lauren K Gadsby, Tyler L Grove, Squire J Booker

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. 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
–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

27 citing papers in PubMed.

  1. Article
  2. Structural and Spectroscopic Basis for Catalysis by a Class C RadicalJournal of the American Chemical Society · 2026
    Article
  3. Structural and Spectroscopic Basis for Catalysis by a Class C RadicalbioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Functional Diversity of HemN-like Proteins.ACS bio & med chem Au · 2022
    Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Methanogenesis marker protein 10 (Mmp10) fromThe Journal of biological chemistry · 2019
    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

6 authors.

Joseph W LaMattinaDepartments of Chemistry and ‡Biochemistry and Molecular Biology, and the §Howard Hughes Medical Institute, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
Bo WangDepartments of Chemistry and ‡Biochemistry and Molecular Biology, and the §Howard Hughes Medical Institute, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
Edward D BaddingDepartments of Chemistry and ‡Biochemistry and Molecular Biology, and the §Howard Hughes Medical Institute, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
Lauren K GadsbyDepartments of Chemistry and ‡Biochemistry and Molecular Biology, and the §Howard Hughes Medical Institute, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
Tyler L GroveDepartments of Chemistry and ‡Biochemistry and Molecular Biology, and the §Howard Hughes Medical Institute, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
Squire J BookerDepartments of Chemistry and ‡Biochemistry and Molecular Biology, and the §Howard Hughes Medical Institute, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.ORCID 0000-0002-7211-5937

Funding

Radical Mechanisms of Iron-Sulfur ProteinsR35GM122595 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SQUIRE J. BOOKER · 2017 to 2026
$3.4M
Radical strategies for inhibiting the antibiotic resistance protein, CfrR21AI111419 · NIAID · PENNSYLVANIA STATE UNIVERSITY, THE · PI BOOKER, SQUIRE J., CHEN, GONG · 2014 to 2015
$398k
Understanding the Biosynthesis of the 2,4-Dimethylindolic Acid Moiety in the Thiopeptide Antibiotic NosiheptideR21AI133318 · NIAID · PENNSYLVANIA STATE UNIVERSITY, THE · PI BOOKER, SQUIRE J. · 2017 to 2018
$347k
NIAID NIH HHS R21 AI111419NIAID NIH HHS R21 AI133318NIGMS NIH HHS R35 GM122595
6 · The paper itself

Abstract

Nosiheptide, a member of the e series of macrocyclic thiopeptide natural products, contains a side-ring system composed of a 3,4-dimethylindolic acid (DMIA) moiety connected to Glu6 and Cys8 of the thiopeptide backbone via ester and thioester linkages, respectively. Herein, we show that NosN, a predicted class C radical S-adenosylmethionine (SAM) methylase, catalyzes both the transfer of a C1 unit from SAM to 3-methylindolic acid linked to Cys8 of a synthetic substrate surrogate as well as the formation of the ester linkage between Glu6 and the nascent C4 methylene moiety of DMIA. In contrast to previous studies that indicated that 5'-methylthioadenosine is the immediate methyl donor in the reaction, in our studies, SAM itself plays this role, giving rise to S-adenosylhomocysteine as a coproduct of the reaction.

Indexed as

MethylationMethyltransferasesS-AdenosylhomocysteineS-AdenosylmethionineThiazolesMethyltransferasesnosiheptideS-AdenosylhomocysteineS-AdenosylmethionineThiazoles

Identifiers

PMID29039940
PMCPMC5938625

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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.