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1
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0030606607
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Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
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Kaneko T, Sato S, Kotani H, Tanaka A, Asamizu E, Nakamura Y, Miyajima N, Hirosawa M, Sugiura M, Sasamolo S, et al.: Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res 1996, 3:109-136.
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(1996)
DNA Res
, vol.3
, pp. 109-136
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Kaneko, T.1
Sato, S.2
Kotani, H.3
Tanaka, A.4
Asamizu, E.5
Nakamura, Y.6
Miyajima, N.7
Hirosawa, M.8
Sugiura, M.9
Sasamolo, S.10
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2
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0029818880
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Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors
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Kehoe DM, Grossman AR: Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors. Science 1996, 273:1409-1412.
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(1996)
Science
, vol.273
, pp. 1409-1412
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Kehoe, D.M.1
Grossman, A.R.2
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3
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0031575895
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A prokaryolic phytochrome
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Hughes J, Lamparter T, Mittmann F, Hartmann E, Gärtner W, Wilde A, Börner T: A prokaryolic phytochrome. Nature 1997, 386:663.
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(1997)
Nature
, vol.386
, pp. 663
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Hughes, J.1
Lamparter, T.2
Mittmann, F.3
Hartmann, E.4
Gärtner, W.5
Wilde, A.6
Börner, T.7
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4
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0030705204
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Characterization of recombinant phytochrome from the cyanobacterium Synechocystis
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Lamparter T, Mittmann F, Gärtner W, Börner T, Hartmann E, Hughes J: Characterization of recombinant phytochrome from the cyanobacterium Synechocystis. Proc Natl Acad Sci USA 1997, 94:11792-11797. See annotation [5•].
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 11792-11797
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Lamparter, T.1
Mittmann, F.2
Gärtner, W.3
Börner, T.4
Hartmann, E.5
Hughes, J.6
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5
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0030865349
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A cyanobacterial phytochrome two-component light sensory system
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Yeh K-C, Wu S-H, Murphy JT, Lagarias JC: A cyanobacterial phytochrome two-component light sensory system. Science 1997, 277:1505-1508. These two papers [4•,5•] describe the isolation and biochemical characterization of the first phytochrome identified in bacteria. The recombinant Synechocystis holoenzyme, expressed in E. coli, was capable of autoassembly in the presence of tetrapyrrole chromophores and had typical phytochrome-like spectral characteristics. Furthermore, Yeh et al. implicate the phytochrome in a light-sensing two-component signaling system by noting that the protein contained a histidine kinase activity and it was able to transfer phosphate to a putative response regulator.
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(1997)
Science
, vol.277
, pp. 1505-1508
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Yeh, K.-C.1
Wu, S.-H.2
Murphy, J.T.3
Lagarias, J.C.4
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6
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0029828327
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Two-component regulatory systems can interact to process multiple environmental signals
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Soncini FC, Groisman EA: Two-component regulatory systems can interact to process multiple environmental signals. J Bacteriol 1996, 178:6796-6801.
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(1996)
J Bacteriol
, vol.178
, pp. 6796-6801
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Soncini, F.C.1
Groisman, E.A.2
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7
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0029816111
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Molecular basis of the magnesium deprivation response in Salmonella typhimurium: Identification of Pho-P regulated genes
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Soncini FC, Véscovi EG, Solomon F, Groisman EA: Molecular basis of the magnesium deprivation response in Salmonella typhimurium: identification of Pho-P regulated genes. J Bacteriol 1996, 178:5092-5099.
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(1996)
J Bacteriol
, vol.178
, pp. 5092-5099
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Soncini, F.C.1
Véscovi, E.G.2
Solomon, F.3
Groisman, E.A.4
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8
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0029671310
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2+ as an extracellular signal: Environmental regulation of Salmonella virulence
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2+ concentrations are <50 μM, PhoQ kinase activity would be high, resulting in activation of the PhoQ/PhoP pathway.
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(1996)
Cell
, vol.84
, pp. 165-174
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Véscovi, E.G.1
Soncini, F.C.2
Groisman, E.A.3
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9
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0029967951
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Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants
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Waldburger CD, Sauer RT: Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants. J Biol Chem 1996, 271:26630-26636.
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(1996)
J Biol Chem
, vol.271
, pp. 26630-26636
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Waldburger, C.D.1
Sauer, R.T.2
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11
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0030925238
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A signal transducer for aerotaxis in Escherichia coli
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Bibikov Sl, Biran R, Rudd KE, Parkinson JS: A signal transducer for aerotaxis in Escherichia coli. J Bacteriol 1997, 179:4075-4079. These two articles [11•, 12•] report the identification of a sensor for aerotaxis (Aer) that allows cells to migrate towards environments containing optimal concentrations of oxygen. The initial identification of Aer, based on the sequence of an open reading frame, is confirmed by a number of genetic and physiological experiments. The protein consists of an amino-terminal cytoplasmic sensing domain homologous to other proteins known to sense oxygen, two transmembrane helices with no intervening periplasmic domain and a carboxy-terminal cytoplasmic signaling domain homologous to those of chemotaxis receptors. Aer was shown to bind FAD [11•]. Tsr, the serine chemoreceptor was also shown to mediate aerotaxis [12•].
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(1997)
J Bacteriol
, vol.179
, pp. 4075-4079
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Bibikov, Sl.1
Biran, R.2
Rudd, K.E.3
Parkinson, J.S.4
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12
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0030883388
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A novel sensor, Aer and the serine chemoreceptor, Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior
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Rebbapragada A, Johnson MS, Harding GP, Zuccarelli AJ, Fletcher HM, Zhulin IB, Taylor BL: A novel sensor, Aer and the serine chemoreceptor, Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior. Proc Natl Acad Sci USA 1997, 94:10541-10546. See annotation [11•].
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 10541-10546
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Rebbapragada, A.1
Johnson, M.S.2
Harding, G.P.3
Zuccarelli, A.J.4
Fletcher, H.M.5
Zhulin, I.B.6
Taylor, B.L.7
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13
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0029875231
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Azobacter vinelandii NifL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch
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Hill S, Austin S, Eydmann T, Jones T, Dixon R: Azobacter vinelandii NifL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch. Proc Natl Acad Sci USA 1996, 93:2143-2148.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 2143-2148
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Hill, S.1
Austin, S.2
Eydmann, T.3
Jones, T.4
Dixon, R.5
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14
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0030884102
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PAS domain S-boxes in Archea, Bacteria and sensors for oxygen and redox
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2 boxes. On the basis of knowledge of the function of these regions in bacterial proteins, the authors suggest that PAS domains may be involved in the sensing of oxygen and redox potential.
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(1997)
Trends Biochem Sci
, vol.22
, pp. 331-333
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Zhulin, I.B.1
Taylor, B.L.2
Dixon, R.3
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15
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0030942247
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Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy
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Lukat-Rodgers GS, Rodgers KR: Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy. Biochemistry 1997, 36:4178-4187.
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(1997)
Biochemistry
, vol.36
, pp. 4178-4187
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Lukat-Rodgers, G.S.1
Rodgers, K.R.2
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16
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0031039158
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The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine
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Mileykovskaya E, Dowhan W: The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine. J Bacteriol 1997, 179:1029-1034.
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(1997)
J Bacteriol
, vol.179
, pp. 1029-1034
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Mileykovskaya, E.1
Dowhan, W.2
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17
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0029853063
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Re-examination of the role of the periplasmic domain of EnvZ in sensing of osmolarity signals in Escherichia coli
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Leonardo MR, Forst S: Re-examination of the role of the periplasmic domain of EnvZ in sensing of osmolarity signals in Escherichia coli. J Bacteriol 1996, 22:405-413. Deletion of various regions throughout the periplasmic domain of the histidine protein kinase EnvZ and replacement of the EnvZ periplasmic domain with the periplasmic domain of PhoR produced proteins that were indistinguishable from wild-type EnvZ in their ability to regulate expression of the outer membrane proteins OmpF and OmpC in response to changes in osmolarity. Interestingly, deletion of the entire periplasmic domain resulted in a protein incapable of osmoregulation, suggesting that although not directly involved in sensing osmolarity, some periplasmic domain or partial domain may be necessary for proper positioning of the transmembrane helices for signaling. The authors suggest that changes in osmalarity, which presumably cause membrane perturbations, are sensed directly through the transmembrane domain of EnvZ and that the periplasmic domain is involved in sensing some other, as yet unidentified, stimulus.
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(1996)
J Bacteriol
, vol.22
, pp. 405-413
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Leonardo, M.R.1
Forst, S.2
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18
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0030606898
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Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis
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Le Moual H, Koshland DE Jr: Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis. J Mol Biol 1996, 261:568-585.
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(1996)
J Mol Biol
, vol.261
, pp. 568-585
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Le Moual, H.1
Koshland D.E., Jr.2
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19
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0029915153
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Imitation of Escherichia coli aspartate receptor signaling in engineered dinners of the cytoplasmic domain
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Cochran AG, Kim PS: Imitation of Escherichia coli aspartate receptor signaling in engineered dinners of the cytoplasmic domain. Science 1996, 271:1113-1116. The cytoplasmic domains of the chemotaxis receptors contain a methylatiori region predicted to exist as an antiparallel coiled-coil attached to a signaling domain that regulates the activity of the histidine protein kinase CheA. These two papers [19•,20•] describe soluble receptor constructs in which leucine zipper motifs were engineered to create dimers of the complete cytoplasmic domain [19•,20•] or of the signaling domain without the methylation region [20•]. Both groups find that these constructs are capable of activating CheA. Interestingly, the most active construct is one that exists as a tetramer [19•]. Cochran and Kim here find that CheA activation can be modulated by adjusting the leucine zipper to twist the receptor dimer interface. This was not observed by Surette and Stock, 1996 [20•], presumably because of inclusion of a flexible linker region between the zipper and the signaling domain. These studies support a model in which signaling is modulated by specific juxtapositioning of signaling domains within the receptor dimer. This contrasts with other studies that show signaling in receptor heterodimers that contain only one cytoplasmic domain [21••,22••].
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(1996)
Science
, vol.271
, pp. 1113-1116
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Cochran, A.G.1
Kim, P.S.2
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20
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0029893940
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Role of alpha-helical coiled-coil interactions in receptor dimerization, signaling, and adaptation during bacterial chemotaxis
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Surette MG, Stock JB: Role of alpha-helical coiled-coil interactions in receptor dimerization, signaling, and adaptation during bacterial chemotaxis. J Biol Chem 1996, 271:17966-17973. See annotation [19•].
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(1996)
J Biol Chem
, vol.271
, pp. 17966-17973
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Surette, M.G.1
Stock, J.B.2
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21
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0029803848
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Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer
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Tatsuno I, Homma M, Oosawa K, Kawagishi I: Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer. Science 1996, 274:423-425. See annotation [22••].
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(1996)
Science
, vol.274
, pp. 423-425
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Tatsuno, I.1
Homma, M.2
Oosawa, K.3
Kawagishi, I.4
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22
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0029851704
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Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain
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Gardina PJ, Manson MD: Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain. Science 1996, 274:425-426. Published together, these papers [21••,22••] describe independent genetic studies of the aspartate chemoreceptor (Tar). Tar, a type I transmembrane receptor, exists and functions as a homodimer. In vivo intersubunit suppression [21••] and intragenic complementation [22••] were used to demonstrate that heterodimers containing only one intact cytoplasmic signaling domain can mediate responses to attractant. This exciting finding sheds new light on the signaling mechanism of type I receptors that were believed to require dimerization for transmembrane signaling activity.
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(1996)
Science
, vol.274
, pp. 425-426
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Gardina, P.J.1
Manson, M.D.2
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23
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0030775629
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Probing the structure of the cytoplasmic domain of the aspartate receptor by targeted disulfide cross-linking
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Chen X, Koshland DE Jr: Probing the structure of the cytoplasmic domain of the aspartate receptor by targeted disulfide cross-linking. Biochemistry 1997, 36:11858-11864.
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(1997)
Biochemistry
, vol.36
, pp. 11858-11864
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Chen, X.1
Koshland D.E., Jr.2
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24
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0030811371
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Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli
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Park H, Inouye M: Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli. J Bacteriol 1997, 179:4382-4390.
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(1997)
J Bacteriol
, vol.179
, pp. 4382-4390
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Park, H.1
Inouye, M.2
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25
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0029779670
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Mutational analysis of a transmembrane segment in a bacterial chemoreceptor
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Baumgartner JW, Hazelbauer GL: Mutational analysis of a transmembrane segment in a bacterial chemoreceptor. J Bacteriol 1996, 178:4651-4660.
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(1996)
J Bacteriol
, vol.178
, pp. 4651-4660
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Baumgartner, J.W.1
Hazelbauer, G.L.2
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26
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0029910912
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Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo
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Hughson AG, Hazelbauer GL: Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo. Proc Natl Acad Sci USA 1996, 93:11546-11551.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 11546-11551
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Hughson, A.G.1
Hazelbauer, G.L.2
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27
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0029865503
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Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
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Chervitz SA, Falke JJ: Molecular mechanism of transmembrane signaling by the aspartate receptor: A model. Proc Natl Acad Sci USA 1996, 93:2545-2550.
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(1996)
Proc Natl Acad Sci USA
, vol.93
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Chervitz, S.A.1
Falke, J.J.2
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28
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0030773005
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Converting a transmembrane receptor to a soluble receptor: Recognition domain to effector domain signaling after excision of the transmembrane domain
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Ottemann KM, Koshland DE Jr: Converting a transmembrane receptor to a soluble receptor: recognition domain to effector domain signaling after excision of the transmembrane domain. Proc Natl Acad Sci USA 1997, 94:11201-11204. The authors report construction of a soluble version of Tar in which the transmembrane segments were removed and the periplasmic and cytoplasmic domains were joined together directly. The resulting construct is functionally very similar to the native receptor in that it can bind aspartate and is capable of signaling, though lacking the transmembrane portion. This very interesting result suggests that putative ligand-induced motions in receptor proteins do not require either transmembrane domains or the membrane itself for transmission of a signal.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 11201-11204
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Ottemann, K.M.1
Koshland D.E., Jr.2
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29
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0029979271
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The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation
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Wu J, Li J, Li G, Long DG, Weis RM: The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation. Biochemistry 1996, 35:4984-4993. The primary site for interaction between the chemotaxis receptor methyltransferase CheR and the receptor was localized to a pentapeptide at the extreme carboxyl termini of some receptors. CheR exhibited similar affinity for receptors and a synthetic pentapeptide with a dissociation constant of approximately 2 μM. The pentapeptide sequence is strictly conserved in the S-typhimurium aspartate receptor and the E. coli aspartate and serine receptors, but lacking in others. This observation, along with numerous other previously published results, is cited by the authors as evidence for a model of intersubunit methylation in which CheR is tethered to one transmembrane receptor from which location it catalyzes methylation of an adjacent receptor. This mechanism of interdimer methylation has been validated by subsequent experimentation [30,31]. This work raises the very interesting possibility that signaling may involve much larger macromolecular complexes than originally envisioned.
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(1996)
Biochemistry
, vol.35
, pp. 4984-4993
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Wu, J.1
Li, J.2
Li, G.3
Long, D.G.4
Weis, R.M.5
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30
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0030768758
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The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process
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Li J, Li G, Weis RM: The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process. Biochemistry 1997, 36:11851-11857.
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(1997)
Biochemistry
, vol.36
, pp. 11851-11857
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Li, J.1
Li, G.2
Weis, R.M.3
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31
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0030736078
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Methylation of the Escherichia coli chemotaxis receptors: Intra- and interdimer mechanisms
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Le Moual H, Quang T, Koshland DE Jr.: Methylation of the Escherichia coli chemotaxis receptors: intra- and interdimer mechanisms. Biochemistry 1997, 36:13441-13448.
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(1997)
Biochemistry
, vol.36
, pp. 13441-13448
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Le Moual, H.1
Quang, T.2
Koshland D.E., Jr.3
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32
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0031569882
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Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine
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Djordjevic S, Stock AM: Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Structure 1997, 5:545-558.
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(1997)
Structure
, vol.5
, pp. 545-558
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Djordjevic, S.1
Stock, A.M.2
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33
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0030595328
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Signal transduction via the multi-step phosphorelay: Not necessarily a road less traveled
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Appleby JL, Parkinson JS, Bourret RB: Signal transduction via the multi-step phosphorelay: not necessarily a road less traveled. Cell 1996, 86:845-848.
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(1996)
Cell
, vol.86
, pp. 845-848
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Appleby, J.L.1
Parkinson, J.S.2
Bourret, R.B.3
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34
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0030984442
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In vitro phosphorylation of the Arc two-component signal transduction system of Escherichia coli
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Georgellis D, Lynch AS, Lin ECC: In vitro phosphorylation of the Arc two-component signal transduction system of Escherichia coli. J Bacteriol 1997, 179:5429-5435. The authors demonstrate the modularity of the ArcBA phosphorelay system by constructing and expressing the individual histidine- and aspartatecontaining phosphotransfer domains. They show that while only one of the domains is capable of autophosphorylation, subsequent phosphotransfer among the various isolated components of the system can occur, but that the favored phosphotransfer reactions follow the four-step phosphorelay circuit as organized within the cell.
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(1997)
J Bacteriol
, vol.179
, pp. 5429-5435
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Georgellis, D.1
Lynch, A.S.2
Lin, E.C.C.3
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35
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0029871035
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Integration of multiple domains in a two-component sensor protein - The Bordetella pertussis BvgAS phosphorelay
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Uhl MA, Miller JF: Integration of multiple domains in a two-component sensor protein - the Bordetella pertussis BvgAS phosphorelay. EMBO J 1996, 15:1028-1036.
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(1996)
EMBO J
, vol.15
, pp. 1028-1036
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Uhl, M.A.1
Miller, J.F.2
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36
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0030466066
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Central role of the BvgS receiver as a phosphorylated intermediate in a complex two-component phosphorelay
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Uhl MA, Miller JF: Central role of the BvgS receiver as a phosphorylated intermediate in a complex two-component phosphorelay. J Biol Chem 1996, 271:33176-33180.
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(1996)
J Biol Chem
, vol.271
, pp. 33176-33180
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Uhl, M.A.1
Miller, J.F.2
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37
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0029941952
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An unorthodox sensor protein (TorS) mediates induction of the for structural genes in response to trimethylamine N-oxide in Escherichia coli
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Jourlin C, Bengrine A, Chippaux M, Mejean V: An unorthodox sensor protein (TorS) mediates induction of the for structural genes in response to trimethylamine N-oxide in Escherichia coli. Mol Microbiol 1996, 20:1297-1306.
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(1996)
Mol Microbiol
, vol.20
, pp. 1297-1306
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Jourlin, C.1
Bengrine, A.2
Chippaux, M.3
Mejean, V.4
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38
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0031564650
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Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli
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Jourlin C, Ansaldi M, Mejean V: Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli. J Mol Biol 1997, 267:770-777.
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(1997)
J Mol Biol
, vol.267
, pp. 770-777
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Jourlin, C.1
Ansaldi, M.2
Mejean, V.3
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39
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0030912553
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New classes of mutants in complementary chromatic adaptation provide evidence for a novel four-step phosphorelay system
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Kehoe DM, Grossman AR: New classes of mutants in complementary chromatic adaptation provide evidence for a novel four-step phosphorelay system. J Bacteriol 1997, 179:3914-3921. The RcaECF system of the filamentous cyanobacterium Fremyella diplosiphon regulates complementary chromatic adaptation. These three proteins are involved In a novel pathway which make use of at least five phospho acceptor domains in the phosphorelay circuit The identification and characterization of this five-step phosphotransfer system points to the increasing diversily of phosphorelay systems currently being found.
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(1997)
J Bacteriol
, vol.179
, pp. 3914-3921
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Kehoe, D.M.1
Grossman, A.R.2
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40
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0030043573
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Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker
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Zhou H, McEvoy MM, Lowry DF, Swanson RV, Simon MI, Dahlquist FW; Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker. Biochemistry 1996, 35:433-443.
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(1996)
Biochemistry
, vol.35
, pp. 433-443
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Zhou, H.1
McEvoy, M.M.2
Lowry, D.F.3
Swanson, R.V.4
Simon, Ml.5
Dahlquist, F.W.6
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41
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0031047030
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Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR
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Zhou H, Dahlquist FW: Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR. Biochemistry 1997, 36:699-710.
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(1997)
Biochemistry
, vol.36
, pp. 699-710
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Zhou, H.1
Dahlquist, F.W.2
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42
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0030940479
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Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB
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Kato M, Mizuno T, Shimizu T, Hakoshima T: Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. Cell 1997, 88:717-723. The X-ray crystal structure of the ArcB histidine-containing phosphotransfer (HPt) domain was determined at 2.06 Å resolution. HPt consists of ∼120 residues and contains a histidine residue involved in phosphotransfer. ArcB HPt exhibits structural homology to the antiparallel four-helix bundle of the CheA autophosphorylation (P1) domain.
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(1997)
Cell
, vol.88
, pp. 717-723
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Kato, M.1
Mizuno, T.2
Shimizu, T.3
Hakoshima, T.4
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43
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0029931125
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Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy
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McEvoy MM, Muhandiram DR, Kay LE, Dahlquist FW: Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. Biochemistry 1996, 35:5633-5640.
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(1996)
Biochemistry
, vol.35
, pp. 5633-5640
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McEvoy, M.M.1
Muhandiram, D.R.2
Kay, L.E.3
Dahlquist, F.W.4
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44
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0031038354
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