Quantitative liquid chromatography–tandem mass spectrometry profiling of activated methyl cycle metabolites involved in LuxS-dependent quorum sensing in Escherichia coli

Halliday, Nigel; Hardie, Kim R.; Williams, Paul; Winzer, Klaus

doi:10.1016/j.ab.2010.04.021

Cited by 53 publications

(51 citation statements)

References 39 publications

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“…SAH is present at ϳ1 M in wild-type E. coli and 50 M in a mutant strain without MTAN (43). Together, these data suggest SAH could have a physiologically relevant role in regulating ThiC activity under conditions where MTAN activity is reduced.…”

Section: Resultsmentioning

confidence: 76%

“…Under normal metabolic conditions, product inhibition would be expected to be minimal. Met concentrations are estimated at 150 -300 M (43,44), and MTAN is present to rapidly hydrolyze low levels of 5Ј-DOA produced. However, these constants suggest that product inhibition could be significant in in vitro assays, including those reported here.…”

Section: ј-Deoxyadenosine and Methionine Cooperatively Inhibitmentioning

confidence: 99%

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The Thiamine Biosynthetic Enzyme ThiC Catalyzes Multiple Turnovers and Is Inhibited by S-Adenosylmethionine (AdoMet) Metabolites

Palmer

Downs

2013

Journal of Biological Chemistry

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Background: ThiC is a radical S-adenosylmethionine (AdoMet) enzyme that synthesizes the thiamine pyrimidine 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P). Results: An increase in the ThiC catalytic rate was detected when product 5Ј-deoxyadenosine was hydrolyzed. ThiC was inhibited by AdoMet metabolites. Conclusion: ThiC is a multiple-turnover enzyme and is product-inhibited. Significance: This is the first report of ThiC catalytic turnover and the identification of two AdoMet metabolites that inhibit ThiC activity.

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Section: Resultsmentioning

confidence: 76%

Section: ј-Deoxyadenosine and Methionine Cooperatively Inhibitmentioning

confidence: 99%

The Thiamine Biosynthetic Enzyme ThiC Catalyzes Multiple Turnovers and Is Inhibited by S-Adenosylmethionine (AdoMet) Metabolites

Palmer

Downs

2013

Journal of Biological Chemistry

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“…The Sgm complex with SAM has a K d of 18 mM (Husain et al 2010), the K d of the RsmC complex with SAM is 5 mM (Sunita et al 2007), and the K d of the RlmI complex with SAM is 3 mM (Sunita et al 2008). This difference might not be very essential for functioning of methyltransferases in vitro, since the intracellular concentration of SAM-400 mM (Halliday et al 2010)-is much greater than the K d for all of these enzymes.…”

Section: Discussionmentioning

confidence: 98%

“…SAM binding was shown to be tightest, with K d = 0.58 mM, while SAH binds four times less tightly, with K d = 2.5 mM. Abundance of SAM in E. coli was estimated to be 400 mM, while that of SAH was 1.3 mM (Halliday et al 2010). Such a difference in binding and metabolite abundance ensures a rapid exchange of SAH to SAM following 30S methylation.…”

Section: Thermodynamic Characteristics Of Rsmd Binding To Sam Sah Amentioning

confidence: 94%

Properties of small rRNA methyltransferase RsmD: Mutational and kinetic study

Sergeeva

Prokhorova²,

Ordabaev³

et al. 2012

RNA

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Ribosomal RNA modification is accomplished by a variety of enzymes acting on all stages of ribosome assembly. Among rRNA methyltransferases of Escherichia coli, RsmD deserves special attention. Despite its minimalistic domain architecture, it is able to recognize a single target nucleotide G966 of the 16S rRNA. RsmD acts late in the assembly process and is able to modify a completely assembled 30S subunit. Here, we show that it possesses superior binding properties toward the unmodified 30S subunit but is unable to bind a 30S subunit modified at G966. RsmD is unusual in its ability to withstand multiple amino acid substitutions of the active site. Such efficiency of RsmD may be useful to complete the modification of a 30S subunit ahead of the 30S subunit's involvement in translation.

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“…AMC is an important metabolic pathway for both prokaryotic and eukaryotic cells. It is responsible for the recycling of sulfur-containing amino acids such as cysteine and homocysteine [Halliday et al, 2010]. S-adenosylmethionine synthase (MetK) converts the abovementioned amino acids to S-adenosylmethionine (SAM), which provides a methyl group for methylation of the proteins, RNA, and DNA.…”

Section: Production Of Signal Moleculesmentioning

confidence: 99%

Molecules Autoinducer 2 and cjA and Their Impact on Gene Expression in <b><i>Campylobacter jejuni</i></b>

et al. 2018

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Quorum sensing is a widespread form of cell-to-cell communication, which is based on the production of signaling molecules known as autoinducers (AIs). The first group contains highly species-specific N-acyl homoserine lactones (N-AHLs), generally known as AI-1, which are produced by AHL synthase. The second group, possessing the characteristic structure of a furanone ring, are known as AI-2. The enzyme responsible for their production is S-ribosylhomocysteine lyase (LuxS). In Campylobacter jejuni, AI-2 and LuxS play a role in many important processes, including biofilm formation, stress response, motility, expression of virulence factors, and colonization. However, neither the receptor protein nor the exact structure of the AI-2 molecule have been identified to date. Similarly, little is known about the possible existence of AHL-synthase producing AI-1 and its impact on gene expression. Recently, an analogue of homoserine lactone, called cjA, was isolated from a cell-free supernatant of C. jejuni strain 81–176 and from the food isolate c11. The molecule cjA particularly impacted the expression of virulence factors and biofilm formation. This review summarizes the role of AI-2 and cjA in the context of biofilm formation, motility, stress responses, and expression of virulence factors.

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Quantitative liquid chromatography–tandem mass spectrometry profiling of activated methyl cycle metabolites involved in LuxS-dependent quorum sensing in Escherichia coli

Cited by 53 publications

References 39 publications

The Thiamine Biosynthetic Enzyme ThiC Catalyzes Multiple Turnovers and Is Inhibited by S-Adenosylmethionine (AdoMet) Metabolites

The Thiamine Biosynthetic Enzyme ThiC Catalyzes Multiple Turnovers and Is Inhibited by S-Adenosylmethionine (AdoMet) Metabolites

Properties of small rRNA methyltransferase RsmD: Mutational and kinetic study

Molecules Autoinducer 2 and cjA and Their Impact on Gene Expression in <b><i>Campylobacter jejuni</i></b>

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