Expression of cspH upon nutrient up-shift in Salmonella enterica serovar typhimurium

• Published in: Archives of microbiology Vol. 182; no. 1; pp. 37 - 43
• Main Authors: Kim, Bae Hoon, Kim, Hyeon Guk, Bae, Gun Ick, Bang, Iel Soo, Bang, Sung Ho, Choi, Jong Hak, Park, Yong Keun
• Format: Journal Article
• Language: English
• Published: Heidelberg Springer 01-09-2004; Berlin Springer Nature B.V
• Subjects: Bacteria; Bacterial Proteins; Bacteriology; Biological and medical sciences; Cold Temperature; Culture Media; Deoxyribonucleic acid; DNA; DNA Gyrase - genetics; DNA Gyrase - isolation & purification; DNA Gyrase - metabolism; Factor For Inversion Stimulation Protein - genetics; Factor For Inversion Stimulation Protein - metabolism; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Bacterial; Heat-Shock Proteins - chemistry; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; Microbiology; Miscellaneous; Nutrients; RNA, Messenger - metabolism; Salmonella; Salmonella enterica; Salmonella typhimurium - genetics; Salmonella typhimurium - metabolism; Temperature; DNA topoisomerase (ATP-hydrolysing); Fis; Isomerases; Microbiology; Enzyme; Nutrient up-shift; cspH; Bacteria; Salmonella typhimurium; DNA gyrase; Enterobacteriaceae
• ISSN: 0302-8933; 1432-072X
• DOI: 10.1007/s00203-004-0692-2

The gene cspH, which encodes one of the cold-shock proteins in Salmonella enterica serovar Typhimurium, has previously been reported to be induced during early exponential phase at 37 degrees C. In the present study, the expression of cspH upon nutrient up-shift at 37 degrees C was investigated and found to be affected by DNA gyrase and DNA-binding protein Fis. When cells at stationary phase were subcultured into a rich medium, the mRNA level of cspH increased dramatically prior to the first cell division. However, when the cells were treated with DNA gyrase inhibitors, cspH mRNA was not induced upon nutrient up-shift. The low level of DNA superhelical density at the cspH promoter in part affected the expression of cspH mRNA in vitro. In addition, a fis-deficient strain had a lower level of cspH mRNA than the wild-type upon nutrient up-shift. Finally, a cspH-lacZ construct, in which the putative binding region for Fis was deleted in the cspH promoter, expressed a low level of LacZ, in contrast to the native cspH-lacZ construct.