title: Influence of RpoN on isocitrate lyase activity in Pseudomonas aeruginosa.
abstract: Pseudomonas aeruginosa is the major aetiological agent of chronic pulmonary infections in patients with cystic fibrosis (CF). The metabolic pathways utilized by P. aeruginosa during these infections, which can persist for decades, are poorly understood. Several lines of evidence suggest that the glyoxylate pathway, which utilizes acetate or fatty acids to replenish intermediates of the tricarboxylic acid cycle, is an important metabolic pathway for P. aeruginosa adapted to the CF lung. Isocitrate lyase (ICL) is one of two major enzymes of the glyoxylate pathway. In a previous study, we determined that P. aeruginosa is dependent upon aceA, which encodes ICL, to cause disease on alfalfa seedlings and in rat lungs. Expression of aceA in PAO1, a P. aeruginosa isolate associated with acute infection, is regulated by carbon sources that utilize the glyoxyate pathway. In contrast, expression of aceA in FRD1, a CF isolate, is constitutively upregulated. Moreover, this deregulation of aceA occurs in other P. aeruginosa isolates associated with chronic infection, suggesting that high ICL activity facilitates adaptation of P. aeruginosa to the CF lung. Complementation of FRD1 with a PAO1 clone bank identified that rpoN negatively regulates aceA. However, the deregulation of aceA in FRD1 was not due to a knockout mutation of rpoN. Regulation of the glyoxylate pathway by RpoN is likely to be indirect, and represents a unique regulatory role for this sigma factor in bacterial metabolism.
authors.affiliation: Department of Biological Sciences, 101 Life Sciences Building, Auburn University, AL 36849, USA.
authors.forename: Jessica M
authors.initials: JM
authors.lastname: Hagins
authors.affiliation: Department of Biological Sciences, 101 Life Sciences Building, Auburn University, AL 36849, USA.
authors.forename: Jessica A
authors.initials: JA
authors.lastname: Scoffield
authors.affiliation: Department of Biological Sciences, 101 Life Sciences Building, Auburn University, AL 36849, USA.
authors.forename: Sang-Jin
authors.initials: SJ
authors.lastname: Suh
authors.affiliation: Department of Biological Sciences, 101 Life Sciences Building, Auburn University, AL 36849, USA.
authors.forename: Laura
authors.initials: L
authors.lastname: Silo-Suh
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003550:Cystic Fibrosis / Q000382:microbiology; D015536:Down-Regulation; D015971:Gene Expression Regulation, Enzymologic; D006038:Glyoxylates / Q000378:metabolism; D006801:Humans; D007522:Isocitrate Lyase / Q000235:genetics / Q000378:metabolism*; D011552:Pseudomonas Infections / Q000382:microbiology*; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D012808:Sigma Factor / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D006038:Glyoxylates; D012808:Sigma Factor; D007522:Isocitrate Lyase