title: Fine-tuning of amino sugar homeostasis by EIIA(Ntr) in Salmonella Typhimurium.
abstract: The nitrogen-metabolic phosphotransferase system, PTS(Ntr), consists of the enzymes I(Ntr), NPr and IIA(Ntr) that are encoded by ptsP, ptsO, and ptsN, respectively. Due to the proximity of ptsO and ptsN to rpoN, the PTS(Ntr) system has been postulated to be closely related with nitrogen metabolism. To define the correlation between PTS(Ntr) and nitrogen metabolism, we performed ligand fishing with EIIA(Ntr) as a bait and revealed that D-glucosamine-6-phosphate synthase (GlmS) directly interacted with EIIA(Ntr). GlmS, which converts D-fructose-6-phosphate (Fru6P) into D-glucosamine-6-phosphate (GlcN6P), is a key enzyme producing amino sugars through glutamine hydrolysis. Amino sugar is an essential structural building block for bacterial peptidoglycan and LPS. We further verified that EIIA(Ntr) inhibited GlmS activity by direct interaction in a phosphorylation-state-dependent manner. EIIA(Ntr) was dephosphorylated in response to excessive nitrogen sources and was rapidly degraded by Lon protease upon amino sugar depletion. The regulation of GlmS activity by EIIA(Ntr) and the modulation of glmS translation by RapZ suggest that the genes comprising the rpoN operon play a key role in maintaining amino sugar homeostasis in response to nitrogen availability and the amino sugar concentration in the bacterial cytoplasm.
authors.affiliation: Department of Food and Animal Biotechnology, Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, and Center for Food and Bioconvergence, Seoul National University, Seoul 08826, Korea.
authors.forename: Woongjae
authors.initials: W
authors.lastname: Yoo
authors.affiliation: Department of Molecular Science and Technology, Department of Applied Chemistry and Biological Engineering, Ajou University, Suwon 16499, Korea.
authors.forename: Hyunjin
authors.initials: H
authors.lastname: Yoon
authors.affiliation: Department of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 08826, Korea.
authors.forename: Yeong-Jae
authors.initials: YJ
authors.lastname: Seok
authors.affiliation: Department of Biological Sciences, Myongji University, Yongin, Gyeonggido 17058, Republic of Korea.
authors.forename: Chang-Ro
authors.initials: CR
authors.lastname: Lee
authors.affiliation: Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Korea.
authors.forename: Hyung Ho
authors.initials: HH
authors.lastname: Lee
authors.affiliation: Department of Food and Animal Biotechnology, Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, and Center for Food and Bioconvergence, Seoul National University, Seoul 08826, Korea.
authors.forename: Sangryeol
authors.initials: S
authors.lastname: Ryu
mesh_terms: D000606:Amino Sugars / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D005636:Fructosephosphates / Q000378:metabolism; D005944:Glucosamine / Q000031:analogs & derivatives / Q000378:metabolism; D019298:Glucose-6-Phosphate / Q000031:analogs & derivatives / Q000378:metabolism; D006706:Homeostasis / Q000502:physiology*; D009584:Nitrogen / Q000378:metabolism; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*; D010766:Phosphorylation / Q000502:physiology; D012486:Salmonella typhimurium / Q000378:metabolism*; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)
chemical_list: D000606:Amino Sugars; D001426:Bacterial Proteins; D005636:Fructosephosphates; D005944:Glucosamine; D019298:Glucose-6-Phosphate; D009584:Nitrogen; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C001293:glucosamine 6-phosphate; C027618:fructose-6-phosphate; C000731191:component S, glutamate mutase protein, Bacteria; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)