title: Autoinducer 2 activity in Escherichia coli culture supernatants can be actively reduced despite maintenance of an active synthase, LuxS.
abstract: Production of the signalling molecule (autoinducer-2) synthesized by LuxS has been proposed to be pivotal to a universal mechanism of inter-species bacterial cell-cell communication (quorum sensing); however recently the function of LuxS has been noted to be integral to central metabolism since it contributes to the activated methyl cycle. This paper shows that when Helicobacter pylori LuxS is overproduced in Escherichia coli, it forms cross-linkable multimers. These multimers persist at comparable levels after 24 h of growth if glucose is omitted from the growth medium; however, the levels of extracellular autoinducer-2 decline (Glucose Retention of AI-2 Levels: GRAIL). Glycerol, maltose, galactose, ribose and L-arabinose could substitute for glucose, but lactose, D-arabinose, acetate, citrate and pyruvate could not. Mutations in (i). metabolic pathways (glycolytic enzymes eno, pgk, pgm; galactose epimerase; the Pta-AckA pathway), (ii). sugar transport (pts components, rbs operon, mgl, trg), and (iii). regulators involved in conventional catabolic repression (crp, cya), cAMP-independent catabolite repression (creC, fruR, rpoS,) the stringent response (relA, spoT) and the global carbon storage regulator (csrA) did not prevent GRAIL. Although the basis of GRAIL remains uncertain, it is clear that the mechanism is distinct from conventional catabolite repression. Moreover, GRAIL is not due to inactivation of the enzymic activity of LuxS, since in E. coli, LuxS contained within stationary-phase cells grown in the absence of glucose maintains its activity in vitro.
authors.affiliation: School of Pharmaceutical Sciences, Nottingham University, Nottingham NG7 2RD, UK.|Institute of Infections and Immunity, Queen's Medical Centre, C-Floor, West Block, Nottingham NG7 2UH, UK.
authors.forename: Kim R
authors.initials: KR
authors.lastname: Hardie
authors.affiliation: Institute of Infections and Immunity, Queen's Medical Centre, C-Floor, West Block, Nottingham NG7 2UH, UK.
authors.forename: Clare
authors.initials: C
authors.lastname: Cooksley
authors.affiliation: School of Pharmaceutical Sciences, Nottingham University, Nottingham NG7 2RD, UK.|Institute of Infections and Immunity, Queen's Medical Centre, C-Floor, West Block, Nottingham NG7 2UH, UK.
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Green
authors.affiliation: Institute of Infections and Immunity, Queen's Medical Centre, C-Floor, West Block, Nottingham NG7 2UH, UK.
authors.forename: Klaus
authors.initials: K
authors.lastname: Winzer
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D013437:Carbon-Sulfur Lyases; D003470:Culture Media; D017077:Culture Media, Conditioned / Q000378:metabolism*; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D005947:Glucose / Q000378:metabolism; D016480:Helicobacter pylori / Q000235:genetics / Q000378:metabolism; D006714:Homoserine / Q000031:analogs & derivatives* / Q000378:metabolism*; D007783:Lactones / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D003470:Culture Media; D017077:Culture Media, Conditioned; D007783:Lactones; C091088:N-octanoylhomoserine lactone; D006714:Homoserine; D013437:Carbon-Sulfur Lyases; C117753:LuxS protein, Bacteria; D005947:Glucose