bioRxivMicrobiologyPreprint
Bacillus licheniformis global nitrogen homeostatic regulator TnrA is a direct repressor of pgsBCAA transcription in Poly-γ-glutamic acid synthesis
Dongbo CaiiD, Yaozhong Chen, Shiyi Wang, Fei Mo, Xin Ma, Shouwen Chen
Abstract
Poly-{gamma}-glutamic acid ({gamma}-PGA) is a multifunctional and naturally occurring biopolymer made from D- and L-glutamate as monomers, which is mainly produced by Bacillus. Few reports have been focused on the regulation network of {gamma}-PGA synthesis in recent years. In this study, we have demonstrated that Bacillus licheniformis global nitrogen homeostatic regulator TnrA is a direct repressor of {gamma}-PGA synthase PgsBCAA in {gamma}-PGA synthesis. First, our results confirmed that TnrA repressed {gamma}-PGA synthesis, deficiency of tnrA led to a 22.03% increase of {gamma}-PGA production, and the {gamma}-PGA yield was decreased by 19.02% in the TnrA overexpression strain. Transcriptional level assay illustrated that the {gamma}-PGA synthase gene cluster pgsBCAA transcriptional level were increased in the tnrA deficient strain WX{Delta}tnrA, indicating that {gamma}-PGA synthase PgsBCAA was negatively regulated by TnrA. Furthermore, electrophoretic mobility shift assay (EMSA) and enzyme expression assays confirmed that TnrA directly repressed pgsBCAA expression by binding to pgsBCAA promoter, and the TnrA-binding site \"CGTCGTCTTCTGTTACA\" in the pgsBCAA promoter was identified by sequence and software analysis. Finally, computer analysis confirmed that the transcription regulations of {gamma}-PGA synthase PgsBCAA by TnrA were highly conserved in other well-studied Bacillus species (B. licheniformis, Bacillus subtilis and Bacillus amyloliquefaciens). Collectively, our results implied that TnrA was a direct repressor for pgsBCAA expression in {gamma}-PGA synthesis, and this research provided a novel regulatory mechanism underlying {gamma}-PGA synthesis, and a new approach that deficiency of tnrA increases {gamma}-PGA production.\n\nImportance{gamma}-PGA is an important biopolymer with many applications, which is mainly produced by Bacillus species. Glutamic acid is the precursor for {gamma}-PGA synthesis, which is catalyzed by the {gamma}-PGA synthase PgsBCAA. Previously, the expression of PgsBCAA was reported to be regulated by ComA-ComP and DegS-DegU, DegQ and SwrA systems, however, few researches were focused on the regulation network of {gamma}-PGA synthesis in recent years. In our research, the {gamma}-PGA synthase PgsBCAA was confirmed to be negatively regulated by the nitrogen metabolism regulator TnrA, and the TnrA binding site in the pgsBCAA promoter was identified in B. licheniformis WX-02. Furthermore, computer analysis implied that TnrA-mediated regulation effect on pgsBCAA expression was highly conserved in Bacillus. Collectively, our research provided a novel regulatory mechanism underlying {gamma}-PGA synthesis, and a new approach that deficiency of tnrA increases {gamma}-PGA production.
- organism: bacteria (other)
- research focus: gene regulatory network inference
- approach: experimental assay
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Metabolomics-assisted mechanism analysis of gamma-PGA synthesis regulated by PhoP in B. licheniformis
- Enhanced Synthesis of Poly Gamma Glutamic Acid by Increasing the Intracellular Reactive Oxygen Species in the Bacillus licheniformis Δ1-pyrroline-5-carboxylate Dehydrogenase Gene ycgN Deficient Strain
- Rewiring central carbon metabolism reveals a trade-off between yield and production rate in poly-γ-glutamic acid synthesis by Bacillus subtilis
Frederik Völker, Michael Kohlstedt, … Lars M. Blank·bioRxiv·Oct 21, 2026
- PgaR is a positive regulator of the pgaABCD biosynthetic operon in Klebsiella pneumoniae
Jonathan Bradshaw, Julia Sanchez‐Garrido, … Gad M. Frankel·Infection and ImmunityPeer-reviewed·Sep 24, 2026
- Truncation of poly-N-acetylglucosamine (PNAG) polymerization with N-acetylglucosamine analogues
Z. Morrison, A. Eddenden, … m. nitz·bioRxiv·Oct 13, 2021
- Characterization of a membrane enzymatic complex for heterologous production of poly-γ-glutamate in E. coli
B. Motta Nascimento, N. U. Nair·bioRxiv·Jul 17, 2020