Analysis of the
            <i>Escherichia coli</i>
            Genome: DNA Sequence of the Region from 84.5 to 86.5 Minutes

Daniels, Donna L.; Plunkett, Guy; Burland, Valerie; Blattner, Frederick R.

doi:10.1126/science.1379743

Cited by 254 publications

(165 citation statements)

References 90 publications

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“…Bioluminescence was measured in V. harveyi strain BB120 (WT) 1 , MM30 (luxS) 14 , BB170 (luxN) 15 , and BB960 (luxQ) 5 . E. coli strains are derivatives of MG1655 16 . The E. coli strains used in Fig.…”

Section: Methodsmentioning

confidence: 99%

Interference with AI-2-mediated bacterial cell–cell communication

Xavier

Bassler

2005

Nature

278

258

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Bacteria communicate with chemical signal molecules called autoinducers. This process, called quorum-sensing, allows bacteria to count the members in the community and to synchronously alter gene expression of the population. Quorum-sensing-controlled processes are often crucial for successful bacterial-host relationships; both symbiotic and pathogenic. Most quorum-sensing autoinducers promote intra-species communication, but one autoinducer, called AI-2, is produced and detected by a wide variety of bacteria and is proposed to allow inter-species communication 1 , 2 . We show here that some species of bacteria can manipulate AI-2 signalling and interfere with other species' ability to correctly assess and respond to changes in cell population density. AI-2-signalling and interference with it could have important ramifications for eukaryotes in maintaining normal microflora and in protection from pathogenic bacteria.The bacterial signal molecule called Autoinducer-2 (AI-2) is a product of the LuxS enzyme which is broadly conserved throughout the bacterial world. LuxS enzymes synthesize 4,5-dihydroxy 2,3-pentanedione (DPD) which undergoes spontaneous rearrangements 3 .Importantly, DPD derivatives interconvert and exist in equilibrium. Different bacteria recognize distinct DPD derivatives, and this family of molecules is generically called AI-2 4 .The interconverting nature of these molecules presumably allows bacteria to respond to their own AI-2 and also to AI-2 produced by other bacterial species, giving rise to the idea that AI-2 represents a universal language fostering inter-species bacterial communication.We characterized the quorum-sensing signal production and detection apparatuses in Vibrio harveyi, Vibrio cholerae, Escherichia coli, and Salmonella typhimurium 5 -8 . In V. harveyi, two autoinducers, AI-1 and AI-2, are detected by LuxN and LuxPQ, respectively, and control expression of genes including those for bioluminescence and Type III secretion (TTS) of virulence factors (Fig. 1a) 5 , 9 . A related quorum-sensing network exists in V. cholerae and controls expression of virulence genes including hapA encoding the haemagglutinin (H/A) protease 6 , 10 .Some bacteria produce and consume AI-2. For example, E. coli and S. typhimurium release AI-2 in exponential phase, and import AI-2 at the transition into stationary phase. This occurs because one target that is activated by AI-2 is the Lsr (for LuxS Regulated) transporter that imports AI-2 (Fig. 1b) 7 , 8 . In the absence of AI-2, LsrR represses the lsr operon. Following AI-2 release, low-level internalization occurs, and intracellular AI-2 is phosphorylated by LsrK 8 , 11 . Phospho-AI-2 (AI-2-P) antagonizes LsrR, which leads to de-repression of lsr expression, assembly of the Lsr transporter, and rapid AI-2 internalization. LsrR -strains are avid AI-2 consumers because the lsr operon is de-repressed. By contrast, LsrK -strains never

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Section: Methodsmentioning

confidence: 99%

Interference with AI-2-mediated bacterial cell–cell communication

Xavier

Bassler

2005

Nature

278

258

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“…Database search with the flavodoxin profile also detects 2 other candidate flavodoxin-like proteins from E. coli, MioC (L~bner-Olesen & Boye, 1992) ( Z score 11) and the hypothetical protein YihB (Daniels et al, 1992) ( Z score 7.8), showing less than 20% sequence identity with each other and with the WrbA family. MioC scores as the best non-flavodoxin sequence of the database.…”

Section: Homology Searchmentioning

confidence: 99%

Six new candidate members of the α/β twisted open‐sheet family detected by sequence similarity to flavodoxin

Grandori

Carey

1994

Protein Science

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We discuss sequence conservation with reference to the known 3-dimensional structures of flavodoxins. Conserved sequence and hydrophobicity patterns, as well as residue-pair interaction potentials, strongly support the hypothesis that these proteins share the a//3 twisted open-sheet fold typical of flavodoxins, with an additional unit in the WrbA family. On the basis of the proposed structural homology, we discuss the details of the putative FMNbinding sites. Our analysis also suggests that the helix-turn-helix motif we identified previously in the C-terminal region of the WrbA family is unlikely to reflect a DNA-binding function of this new protein family.

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“…2): one group collects the K258-containing putative aminotransferases, the second the PMP-dependent dehydrases containing the histidine, and the third coincides with YIFI-ECOLI, which has K258 but other peculiarities not yet well understood. Dhillon et al, 1989Takagi et al, 1990Stutzman-Engwall et al, 1992Lacalle et al, 1992Distler et al, 1992Jiang et al, 1991Daniels et al, 1992Thorson et al, 1993Thorson et al, 1993 a Available SWISS-PROT codes.…”

Section: Y H G V S L W a E R L S Q E L L A L P S H P G L H L D Hmentioning

confidence: 99%

Similarity between pyridoxal/pyridoxamine phosphate‐dependent enzymes involved in dideoxy and deoxyaminosugar biosynthesis and other pyridoxal phosphate enzymes

Pascarella¹,

Bossa²

1994

Protein Science

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A multiple sequence alignment among aspartate aminotransferase, dialkylglycine decarboxylase, and serine hydroxymethyltransferase (DAS) was used for profile databank search.The DAS profile could detect similarities to other pyridoxal or pyridoxamine phosphate-dependent enzymes, like several gene products involved in dideoxysugar and deoxyaminosugar synthesis. The alignment among DAS and such gene products shows the conservation of aspartate 222 and lysine 258, which, in aspartate aminotransferase, interacts with the N1 of the coenzyme pyridine ring and forms the internal Schiff base, respectively. The lysine is replaced by histidine in the pyridoxamine phosphate-dependent gene products. The alignment indicates also that the region encompassing the coenzyme binding site is the most conserved.

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Analysis of the Escherichia coli Genome: DNA Sequence of the Region from 84.5 to 86.5 Minutes

Cited by 254 publications

References 90 publications

Interference with AI-2-mediated bacterial cell–cell communication

Interference with AI-2-mediated bacterial cell–cell communication

Six new candidate members of the α/β twisted open‐sheet family detected by sequence similarity to flavodoxin

Similarity between pyridoxal/pyridoxamine phosphate‐dependent enzymes involved in dideoxy and deoxyaminosugar biosynthesis and other pyridoxal phosphate enzymes

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