ArticleJournal of the American Chemical Society2015
Identification of an Auxiliary Leader Peptide-Binding Protein Required for Azoline Formation in Ribosomal Natural Products.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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.
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.
Who cites it
36 citing papers in PubMed, 60 citations in OpenAlex.
- Structural basis for iterative methylation by a cobalamin-dependent radicalProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural Basis for Iterative Methylation by a Cobalamin-dependent Radical S-Adenosylmethionine Enzyme in Cystobactamids Biosynthesis.bioRxiv : the preprint server for biology · 2025Article
- ThiF-Like Enzyme Chemistry in Primary and Secondary Metabolism.Chembiochem : a European journal of chemical biology · 2025Review
- Characterizing and engineering post-translational modifications with high-throughput cell-free expression.Nature communications · 2025Article
- Assessing Substrate Scope of the Cyclodehydratase LynD by mRNA Display-Enabled Machine Learning Models.Biochemistry · 2025Article
- Indolylamide Macrocyclization by aOrganic letters · 2025Article
- Biosynthesis of peptide-nucleobase hybrids in ribosomal peptides.Nature chemical biology · 2025Article
- Structural Evidence for DUF512 as a RadicalACS bio & med chem Au · 2024Article
- Article
- Micrococcin cysteine-to-thiazole conversion through transient interactions between the scaffolding protein TclI and the modification enzymes TclJ and TclN.Applied and environmental microbiology · 2024Article
- Microbial synthesis of pyrroloquinoline quinone.World journal of microbiology & biotechnology · 2023Review
- Cell-free Biosynthesis of Peptidomimetics.Biotechnology and bioprocess engineering : BBE · 2023Review
- Bioinformatic prediction and experimental validation of RiPP recognition elements.Methods in enzymology · 2023Article
- Functional elucidation of TfuA in peptide backbone thioamidation.Nature chemical biology · 2021Article
- Enzymatic thioamidation of peptide backbones.Methods in enzymology · 2021Article
- Global Genome Mining Reveals the Distribution of Diverse Thioamidated RiPP Biosynthesis Gene Clusters.Frontiers in microbiology · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Article
- Substrate Recognition by the Class II Lanthipeptide Synthetase HalM2.ACS chemical biology · 2020Article
- Translation-Targeting RiPPs and Where to Find Them.Frontiers in genetics · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Thiazole/oxazole-modified microcins (TOMMs) are a class of post-translationally modified peptide natural products bearing azole and azoline heterocycles. The first step in heterocycle formation is carried out by a two component cyclodehydratase comprised of an E1 ubiquitin-activating and a YcaO superfamily member. Recent studies have demonstrated that the YcaO domain is responsible for cyclodehydration, while the TOMM E1 homologue is responsible for peptide recognition during azoline formation. Although all characterized TOMM biosynthetic clusters contain this canonical TOMM E1 homologue (C domain), we also identified a second, highly divergent E1 superfamily member, annotated as an Ocin-ThiF-like protein (F protein), associated with more than 300 TOMM biosynthetic clusters. Here we describe the in vitro reconstitution of a novel TOMM cyclodehydratase from such a cluster and demonstrate that this auxiliary protein is required for cyclodehydration. Using a combination of biophysical techniques, we demonstrate that the F protein, rather than the C domain, is responsible for engaging the peptide substrate. The C domain instead appears to serve as a scaffolding protein, bringing the catalytic YcaO domain and the peptide binding Ocin-ThiF-like protein into proximity. Our findings provide an updated biosynthetic framework that provides a foundation for the characterization and reconstitution of approximately 25% of bioinformatically identifiable TOMM synthetases.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.