Evidence map›Paper›PMID 34504067›Full record

ArticleNature communications2021

Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis.

Fredarla S Miller, Kathryn K Crone, Matthew R Jensen, Sudipta Shaw, William R Harcombe, Mikael H Elias, Michael F Freeman

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
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  6. Genome Mining and Biological Engineering of Type III Borosins from Bacteria.International journal of molecular sciences · 2024
    Article
  7. Article
  8. Article
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  11. Review
  12. Article
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  14. Peptides hit the catalysis walk.Nature chemical biology · 2023
    Article
  15. Review
  16. Article
  17. Review
  18. Article
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  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

7 authors at 1 institution in 1 country.

Fredarla S Miller *Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota-Twin Cities, St. Paul, MN, USA.ORCID 0000-0002-6948-3683
Kathryn K Crone *Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota-Twin Cities, St. Paul, MN, USA.ORCID 0000-0001-9888-4710
Matthew R JensenBioTechnology Institute, University of Minnesota-Twin Cities, St. Paul, MN, USA.ORCID 0000-0001-5469-1239
Sudipta ShawDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota-Twin Cities, St. Paul, MN, USA.
William R HarcombeBioTechnology Institute, University of Minnesota-Twin Cities, St. Paul, MN, USA.ORCID 0000-0001-8445-2052
Mikael H EliasDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota-Twin Cities, St. Paul, MN, USA. mhelias@umn.edu.
Michael F FreemanDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota-Twin Cities, St. Paul, MN, USA. mffreema@umn.edu.ORCID 0000-0002-0491-9618
University of Minnesota · US

Funding

Discovery and characterization of biocatalysts for ribosomally encoded alpha-N-methylated peptide natural productsR35GM133475 · NIGMS · UNIVERSITY OF MINNESOTA · PI Michael F Freeman · 2019 to 2026
$2.7M
NIGMS NIH HHS R35 GM133475
6 · The paper itself

Abstract

Peptide backbone α-N-methylations change the physicochemical properties of amide bonds to provide structural constraints and other favorable characteristics including biological membrane permeability to peptides. Borosin natural product pathways are the only known ribosomally encoded and posttranslationally modified peptides (RiPPs) pathways to incorporate backbone α-N-methylations on translated peptides. Here we report the discovery of type IV borosin natural product pathways (termed 'split borosins'), featuring an iteratively acting α-N-methyltransferase and separate precursor peptide substrate from the metal-respiring bacterium Shewanella oneidensis. A series of enzyme-precursor complexes reveal multiple conformational states for both α-N-methyltransferase and substrate. Along with mutational and kinetic analyses, our results give rare context into potential strategies for iterative maturation of RiPPs.

Indexed as

Protein Processing, Post-TranslationalAlgorithmsBacterial ProteinsBinding SitesBiological ProductsCrystallography, X-RayKineticsMethylationMethyltransferasesMutationPeptidesProtein ConformationProtein MultimerizationRibosomesShewanellaSubstrate SpecificityBacterial ProteinsBiological ProductsMethyltransferasesPeptides

Identifiers

PMID34504067
PMCPMC8429565
OpenAlexW3192550194

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.