title: SspA is required for acid resistance in stationary phase by downregulation of H-NS in Escherichia coli.
abstract: The stringent starvation protein A (SspA) is a RNA polymerase-associated protein and is required for transcriptional activation of bacteriophage P1 late promoters. However, the role of SspA in gene expression in Escherichia coli is essentially unknown. In this work, we show that SspA is essential for cell survival during acid-induced stress. Apparently, SspA inhibits stationary-phase accumulation of H-NS, a global regulator which functions mostly as a repressor, thereby derepressing multiple stress defence systems including those for acid stress and nutrient starvation. Consequently, the gene expression pattern of the H-NS regulon is altered in the sspA mutant, leading to acid-sensitive and hypermotile phenotypes. Thus, our study indicates that SspA is a global regulator, which acts upstream of H-NS, and thereby plays an important role in the stress response of E. coli during stationary phase. In addition, our results indicate that the expression of the H-NS regulon is sensitive to small changes in the cellular level of H-NS, enabling the cell to response rapidly to environment cues. As SspA and H-NS are highly conserved among Gram-negative bacteria, of which many are pathogenic, the global role of SspA in the stress response and pathogenesis is discussed.
authors.affiliation: Transcription Control Section, Gene Regulation and Chromosome Biology Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, NIH, Bldg. 469, PO Box B, Frederick, MD 21702, USA.
authors.forename: Anne-Marie
authors.initials: AM
authors.lastname: Hansen
authors.forename: Yu
authors.initials: Y
authors.lastname: Qiu
authors.forename: Norman
authors.initials: N
authors.lastname: Yeh
authors.forename: Frederick R
authors.initials: FR
authors.lastname: Blattner
authors.forename: Tim
authors.initials: T
authors.lastname: Durfee
authors.forename: Ding Jun
authors.initials: DJ
authors.lastname: Jin
mesh_terms: D000143:Acids / Q000494:pharmacology; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D015536:Down-Regulation; D024881:Drug Resistance, Bacterial / Q000235:genetics*; D004926:Escherichia coli / Q000187:drug effects / Q000254:growth & development / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects; D006090:Gram-Negative Bacteria / Q000235:genetics / Q000472:pathogenicity; D008969:Molecular Sequence Data; D009154:Mutation; D010802:Phylogeny; D012323:RNA Processing, Post-Transcriptional; D017386:Sequence Homology, Amino Acid; D012808:Sigma Factor / Q000235:genetics / Q000378:metabolism
chemical_list: D000143:Acids; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C031908:H-NS protein, bacteria; D012808:Sigma Factor; C072071:SspA protein, E coli; C069567:sigma factor KatF protein, Bacteria