作者: Linda I. Hu , Ekaterina V. Filippova , Joseph Dang , Sergii Pshenychnyi , Jiapeng Ruan
DOI: 10.1371/JOURNAL.PONE.0207563
关键词: Small RNA 、 Protein Data Bank (RCSB PDB) 、 Transcription factor 、 Transcription (biology) 、 Cell biology 、 RNA 、 Spermidine 、 Acetyltransferase 、 Response regulator 、 Chemistry
摘要: Spermidine N-acetyltransferase (SpeG) acetylates and thus neutralizes toxic polyamines. Studies indicate that SpeG plays an important role in virulence pathogenicity of many bacteria, which have evolved SpeG-dependent strategies to control polyamine concentrations survive their hosts. In Escherichia coli, the two-component response regulator RcsB is reported be subject Ne-acetylation on several lysine residues, resulting reduced DNA binding affinity transcription small RNA rprA; however, physiological acetylation mechanism responsible for this behavior has not been fully determined. Here, we performed acetyltransferase screen found inhibits rprA promoter activity acetylation-independent manner. Surface plasmon resonance analysis revealed can physically interact with DNA-binding carboxyl domain RcsB. We hypothesize interacts interaction might inhibition RcsB-dependent transcription. This work provides a model as modulator E. coli through its ability factor first study provide evidence enzyme involved metabolism influence function global RcsB, integrates information concerning envelope stresses central metabolic status regulate diverse behaviors.