| Title | Rewiring of the FtsH regulatory network by a single nucleotide change in saeS of Staphylococcus aureus |
| Authors | Liu, Qian Hu, Mo Yeo, Won-Sik He, Lei Li, Tianming Zhu, Yuanjun Meng, Hongwei Wang, Yanan Lee, Hyunwoo Liu, Xiaoyun Li, Min Bae, Taeok |
| Affiliation | Shanghai Jiao Tong Univ, Sch Med, Ren Ji Hosp, Dept Lab Med, Shanghai 200127, Peoples R China. Peking Univ, Insy Analyt Chem, Coll Chem & Mol Engn, Beijing 100871, Peoples R China. Peking Univ, Synthet & Funct Biomol Ctr, Coll Chem & Mol Engn, Beijing 100871, Peoples R China. Indiana Univ Sch Med Northwest, Dept Microbiol & Immunol, Gary, IN 46408 USA. Univ Illinois, Coll Pharm, Dept Biopharmaceut Sci, Chicago, IL 60607 USA. Univ Illinois, Coll Pharm, Ctr Biomol Sci, Chicago, IL 60607 USA. Johnson Med Co Adv Energy, Shanghai 200233, Peoples R China. Shanghai Jiao Tong Univ, Sch Med, Ren Ji Hosp, Dept Lab Med, Shanghai 200127, Peoples R China. Liu, XY (reprint author), Peking Univ, Insy Analyt Chem, Coll Chem & Mol Engn, Beijing 100871, Peoples R China. Liu, XY (reprint author), Peking Univ, Synthet & Funct Biomol Ctr, Coll Chem & Mol Engn, Beijing 100871, Peoples R China. Bae, T (reprint author), Indiana Univ Sch Med Northwest, Dept Microbiol & Immunol, Gary, IN 46408 USA. |
| Keywords | SENSOR KINASE SAES AAA PROTEASE FTSH ESCHERICHIA-COLI 2-COMPONENT SYSTEM MEMBRANE-PROTEINS PLASMA-MEMBRANE PROTEOLYTIC ACTIVITY COMPLEX LOCUS SECY |
| Issue Date | 2017 |
| Publisher | SCIENTIFIC REPORTS |
| Citation | SCIENTIFIC REPORTS.2017,7. |
| Abstract | In the Gram-positive pathogen Staphylococcus aureus, the membrane-bound ATP-dependent metalloprotease FtsH plays a critical role in resistance to various stressors. However, the molecular mechanism of the FtsH functions is not known. Here, we identified core FtsH target proteins in S. aureus. In the strains Newman and USA300, the abundance of 33 proteins were altered in both strains, of which 11 were identified as core FtsH substrate protein candidates. In the strain Newman and some other S. aureus strains, the sensor histidine kinase SaeS has an L18P (T53C in saeS) substitution, which transformed the protein into an FtsH substrate. Due to the increase of SaeS L18P in the ftsH mutant, Eap, a sae-regulon protein, was also increased in abundance, causing the Newman-specific cell-aggregation phenotype. Regardless of the strain background, however, the ftsH mutants showed lower virulence and survival in a murine infection model. Our study illustrates the elasticity of the bacterial regulatory network, which can be rewired by a single substitution mutation. |
| URI | http://hdl.handle.net/20.500.11897/471447 |
| ISSN | 2045-2322 |
| DOI | 10.1038/s41598-017-08774-5 |
| Indexed | SCI(E) |
| Appears in Collections: | å å¦ä¸ å å å·¥ç¨ å¦é ¢ |
