Bacillus Subtilis Rifampicin Phosphorylation and Resistance Study

A 1.2 MB PDF research article by Šárka Bobková, published on figshare in April 2026, investigates the evolutionary link between bacterial phosphotransferase systems and rifampicin-inactivating enzymes. The study provides biochemical evidence using Bacillus subtilis strains, growth assays, and liquid chromatography-mass spectrometry to demonstrate rifampicin phosphorylation.

Use Cases

• Analyze the impact of ptsH, ptsI, and rphT gene deletions on Bacillus subtilis growth in the presence of rifampicin.
• Study in vitro phosphorylation of rifampicin by the PTS complex components HPr, EI, MtlF, and PckA.
• Evaluate the role of the protein EI in rifampicin phosphorylation activity.
• Investigate the conferral of high-level rifampicin resistance through heterologous expression of the rphT gene.
• Examine protein–rifampicin interaction data characterized via thermophoresis assays.

Strengths

• Primary research data from controlled laboratory experiments on Bacillus subtilis strains.
• Study employs multiple validation methods: growth assays, liquid chromatography-mass spectrometry, and thermophoresis.

Limitations

• Small dataset scale at 1.2 MB, containing a single research article without underlying raw data tables.
• Temporal coverage and sample size for experimental replicates are not specified in the provided description.
• Geographic and species coverage is limited to the laboratory study of Bacillus subtilis.

Provenance

Source

Šárka Bobková via figshare.

Collection Method

Laboratory experiments including gene deletion, growth assays, liquid chromatography-mass spectrometry, and thermophoresis.

Time Range

Study period not specified; publication date is 2026.

Freshness

Last updated April 2026.

Geography

Laboratory study, specific location not provided.