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Peer-reviewedCC BY 4.0Science Advances

Direct regulation of a tRNA modification enzyme by ppGpp links stress signaling to translational control and biofilm development

  • Aude E. Trinquier1
  • Franck Slama2
  • Junlang Liu3
  • Lucille Pham1
  • Lauren Stolt1
  • Jue D. Wang1
  1. 1Department of Bacteriology, University of Wisconsin-Madison, Madison, WI 53706, USA.
  2. 2Independent researcher, Madison, WI, USA.
  3. 3Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
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Abstract

Transfer RNA (tRNA) modifications influence decoding efficiency and translational fidelity, yet how they are integrated into bacterial signaling networks remains poorly understood. Here, we identify a direct connection between stress signaling and codon-specific translational regulation. We show that the alarmone guanosine tetraphosphate (ppGpp) directly inhibits MnmE (TrmE), a conserved tRNA-modification GTPase required for methylaminomethyl (mnm) modification of wobble uridine. High-resolution ribosome profiling in Bacillus subtilis revealed that loss of MnmE selectively increases ribosome pausing at AAG codons and reprograms translation of a subset of genes, including small open reading frames. Among these is a previously unrecognized AAG-containing leader peptide that controls expression of the biofilm repressor AbrB. Consistent with this mechanism, mnmE mutants exhibit constitutive extracellular matrix production and bypass the biofilm defect of a relA mutant. Together, these findings establish a pathway linking ppGpp signaling, tRNA modification, codon-specific translation, and multicellular development.

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Cite

BibTeXRIS
BibTeX
@article{trinquier2026direct,
  title = {{Direct regulation of a tRNA modification enzyme by ppGpp links stress signaling to translational control and biofilm development}},
  author = {Aude E. Trinquier and Franck Slama and Junlang Liu and Lucille Pham and Lauren Stolt and Jue D. Wang},
  journal = {Science Advances},
  year = {2026},
  month = nov,
  doi = {10.1126/sciadv.aek6976},
  url = {https://www.science.org/doi/abs/10.1126/sciadv.aek6976},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Direct regulation of a tRNA modification enzyme by ppGpp links stress signaling to translational control and biofilm development
AU  - Aude E. Trinquier
AU  - Franck Slama
AU  - Junlang Liu
AU  - Lucille Pham
AU  - Lauren Stolt
AU  - Jue D. Wang
PY  - 2026
DA  - 2026/11/04
JO  - Science Advances
DO  - 10.1126/sciadv.aek6976
UR  - https://www.science.org/doi/abs/10.1126/sciadv.aek6976
AB  - Transfer RNA (tRNA) modifications influence decoding efficiency and translational fidelity, yet how they are integrated into bacterial signaling networks remains poorly understood. Here, we identify a direct connection between stress signaling and codon-specific translational regulation. We show that the alarmone guanosine tetraphosphate (ppGpp) directly inhibits MnmE (TrmE), a conserved tRNA-modification GTPase required for methylaminomethyl (mnm) modification of wobble uridine. High-resolution ribosome profiling in Bacillus subtilis revealed that loss of MnmE selectively increases ribosome pausing at AAG codons and reprograms translation of a subset of genes, including small open reading frames. Among these is a previously unrecognized AAG-containing leader peptide that controls expression of the biofilm repressor AbrB. Consistent with this mechanism, mnmE mutants exhibit constitutive extracellular matrix production and bypass the biofilm defect of a relA mutant. Together, these findings establish a pathway linking ppGpp signaling, tRNA modification, codon-specific translation, and multicellular development.
SN  - 2375-2548
ER  -