Evidence map›Paper›PMID 41538315›Full record

ArticleNucleic acids research2026

TlyA is a 23S and 16S 2'-O-methylcytidine methyltransferase important for ribosome assembly in Bacillus subtilis.

Jennie L Hibma, Lia M Munson, Joshua D Jones, Taylor M Nye, Kristin S Koutmou, Lyle A Simmons

Abstract read
In one paragraph

Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Jennie L HibmaDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, United States.
Lia M MunsonDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, United States.
Joshua D JonesDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, United States.
Taylor M NyeDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, United States.
Kristin S KoutmouDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, United States.
Lyle A SimmonsDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, United States.ORCID 0000-0002-9600-7623

Funding

PREDOCTORAL TRAINING IN GENETICST32GM007544 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORAN, JOHN V. · 1985 to 2022
$11.3M
Novel mechanisms of DNA repair and cell cycle regulation in bacteriaR35GM131772 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Lyle Simmons · 2019 to 2026
$2.8M
MFB: Integrating LC-MS/MS and Nanopore Sequencing Platforms to Enable the Direct and Quantatative Detection of RNA ModificationsR01HG013876 · NHGRI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Kristin S Koutmou · 2024 to 2026
$1.2M
Genetics Training Program T32-GM007544NHGRI NIH HHS R01 HG013876NIGMS NIH HHS R35 GM131772NIGMS NIH HHS T32 GM007544NIH HHS R01HG013876NIH HHS R35GM131772
6 · The paper itself

Abstract

Ribosomal RNA (rRNA) methylation is conserved across biology, yet the effect of rRNA methylation on ribosome function is poorly understood. In this work, we identify a biological function for the rRNA 2'-O-methylcytidine methyltransferase TlyA, conserved between Bacillus subtilis and Mycobacterium tuberculosis (Mtb). The tlyA deletion in B. subtilis confers a cold sensitive phenotype and resistance to aminoglycoside and cyclic polypeptide antibiotics. We show that ∆tlyA cells have ribosome assembly defects characterized by accumulation of the 50S subunit. Using a genetic approach, we tested the importance of potential catalytic residues and S-adenosyl-l-methionine (SAM) cofactor binding sites identified based on sequence alignments with other rRNA methyltransferases. We show that B. subtilis TlyA uses the common rRNA methyltransferase catalytic triad KDK and SAM binding motif GxSxG. This differs from TlyA from Mtb, which requires an additional tetrapeptide linker. Together our work demonstrates that B. subtilis tlyA is critical for ribosome assembly and we identify key residues for TlyA function in vivo. Since Escherichia coli lacks TlyA or a functional equivalent, our work highlights key differences in ribosome maturation between B. subtilis, Mtb, and more divergent Gram-negative bacteria providing new insight into rRNA maturation and antibiotic resistance mechanisms.

Indexed as

Bacillus subtilisBacterial ProteinsMethyltransferasesRibosomesRNA, Ribosomal, 16SRNA, Ribosomal, 23SBinding SitesRNA MethylationS-AdenosylmethionineBacterial ProteinsMethyltransferasesRNA, Ribosomal, 16SRNA, Ribosomal, 23SS-Adenosylmethionine

Identifiers

PMID41538315
PMCPMC12805891

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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.