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Autoinducer 2 activity in Escherichia coli culture supernatants can be actively reduced despite maintenance of an active synthase, LuxS.

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Autoinducer 2 activity in Escherichia coli culture supernatants can be actively reduced despite maintenance of an active synthase, LuxS. / Hardie, Kim R.; Cooksley, Clare; Green, Andrew D. et al.
In: Microbiology, Vol. 149, No. 3, 03.2003, p. 715-728.

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Hardie KR, Cooksley C, Green AD, Winzer K. Autoinducer 2 activity in Escherichia coli culture supernatants can be actively reduced despite maintenance of an active synthase, LuxS. Microbiology. 2003 Mar;149(3):715-728. doi: 10.1099/mic.0.25853-0

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Hardie, Kim R. ; Cooksley, Clare ; Green, Andrew D. et al. / Autoinducer 2 activity in Escherichia coli culture supernatants can be actively reduced despite maintenance of an active synthase, LuxS. In: Microbiology. 2003 ; Vol. 149, No. 3. pp. 715-728.

Bibtex

@article{2b429c96c1fb4e03bab03b982d66ef5f,
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.",
author = "Hardie, {Kim R.} and Clare Cooksley and Green, {Andrew D.} and Klaus Winzer",
year = "2003",
month = mar,
doi = "10.1099/mic.0.25853-0",
language = "English",
volume = "149",
pages = "715--728",
journal = "Microbiology",
issn = "1350-0872",
publisher = "Society for General Microbiology",
number = "3",

}

RIS

TY - JOUR

T1 - Autoinducer 2 activity in Escherichia coli culture supernatants can be actively reduced despite maintenance of an active synthase, LuxS.

AU - Hardie, Kim R.

AU - Cooksley, Clare

AU - Green, Andrew D.

AU - Winzer, Klaus

PY - 2003/3

Y1 - 2003/3

N2 - 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.

AB - 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.

U2 - 10.1099/mic.0.25853-0

DO - 10.1099/mic.0.25853-0

M3 - Journal article

VL - 149

SP - 715

EP - 728

JO - Microbiology

JF - Microbiology

SN - 1350-0872

IS - 3

ER -