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Volumn 1, Issue 2, 1998, Pages 160-169

Signal transduction in bacteria: Molecular mechanisms of stimulus-response coupling

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 0032034821     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(98)80006-4     Document Type: Article
Times cited : (44)

References (82)
  • 1
    • 0030606607 scopus 로고    scopus 로고
    • 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
    • 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.
    • (1996) DNA Res , vol.3 , pp. 109-136
    • 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
  • 2
    • 0029818880 scopus 로고    scopus 로고
    • Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors
    • Kehoe DM, Grossman AR: Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors. Science 1996, 273:1409-1412.
    • (1996) Science , vol.273 , pp. 1409-1412
    • Kehoe, D.M.1    Grossman, A.R.2
  • 5
    • 0030865349 scopus 로고    scopus 로고
    • A cyanobacterial phytochrome two-component light sensory system
    • 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.
    • (1997) Science , vol.277 , pp. 1505-1508
    • Yeh, K.-C.1    Wu, S.-H.2    Murphy, J.T.3    Lagarias, J.C.4
  • 6
    • 0029828327 scopus 로고    scopus 로고
    • Two-component regulatory systems can interact to process multiple environmental signals
    • Soncini FC, Groisman EA: Two-component regulatory systems can interact to process multiple environmental signals. J Bacteriol 1996, 178:6796-6801.
    • (1996) J Bacteriol , vol.178 , pp. 6796-6801
    • Soncini, F.C.1    Groisman, E.A.2
  • 7
    • 0029816111 scopus 로고    scopus 로고
    • Molecular basis of the magnesium deprivation response in Salmonella typhimurium: Identification of Pho-P regulated genes
    • 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.
    • (1996) J Bacteriol , vol.178 , pp. 5092-5099
    • Soncini, F.C.1    Véscovi, E.G.2    Solomon, F.3    Groisman, E.A.4
  • 8
    • 0029671310 scopus 로고    scopus 로고
    • 2+ as an extracellular signal: Environmental regulation of Salmonella virulence
    • 2+ concentrations are <50 μM, PhoQ kinase activity would be high, resulting in activation of the PhoQ/PhoP pathway.
    • (1996) Cell , vol.84 , pp. 165-174
    • Véscovi, E.G.1    Soncini, F.C.2    Groisman, E.A.3
  • 9
    • 0029967951 scopus 로고    scopus 로고
    • Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants
    • 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.
    • (1996) J Biol Chem , vol.271 , pp. 26630-26636
    • Waldburger, C.D.1    Sauer, R.T.2
  • 11
    • 0030925238 scopus 로고    scopus 로고
    • A signal transducer for aerotaxis in Escherichia coli
    • 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•].
    • (1997) J Bacteriol , vol.179 , pp. 4075-4079
    • Bibikov, Sl.1    Biran, R.2    Rudd, K.E.3    Parkinson, J.S.4
  • 12
    • 0030883388 scopus 로고    scopus 로고
    • 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
    • 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•].
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10541-10546
    • 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
  • 13
    • 0029875231 scopus 로고    scopus 로고
    • Azobacter vinelandii NifL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch
    • 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.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2143-2148
    • Hill, S.1    Austin, S.2    Eydmann, T.3    Jones, T.4    Dixon, R.5
  • 14
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in Archea, Bacteria and sensors for oxygen and redox
    • 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.
    • (1997) Trends Biochem Sci , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3
  • 15
    • 0030942247 scopus 로고    scopus 로고
    • Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy
    • Lukat-Rodgers GS, Rodgers KR: Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy. Biochemistry 1997, 36:4178-4187.
    • (1997) Biochemistry , vol.36 , pp. 4178-4187
    • Lukat-Rodgers, G.S.1    Rodgers, K.R.2
  • 16
    • 0031039158 scopus 로고    scopus 로고
    • The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine
    • 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.
    • (1997) J Bacteriol , vol.179 , pp. 1029-1034
    • Mileykovskaya, E.1    Dowhan, W.2
  • 17
    • 0029853063 scopus 로고    scopus 로고
    • Re-examination of the role of the periplasmic domain of EnvZ in sensing of osmolarity signals in Escherichia coli
    • 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.
    • (1996) J Bacteriol , vol.22 , pp. 405-413
    • Leonardo, M.R.1    Forst, S.2
  • 18
    • 0030606898 scopus 로고    scopus 로고
    • Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis
    • 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.
    • (1996) J Mol Biol , vol.261 , pp. 568-585
    • Le Moual, H.1    Koshland D.E., Jr.2
  • 19
    • 0029915153 scopus 로고    scopus 로고
    • Imitation of Escherichia coli aspartate receptor signaling in engineered dinners of the cytoplasmic domain
    • 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••].
    • (1996) Science , vol.271 , pp. 1113-1116
    • Cochran, A.G.1    Kim, P.S.2
  • 20
    • 0029893940 scopus 로고    scopus 로고
    • Role of alpha-helical coiled-coil interactions in receptor dimerization, signaling, and adaptation during bacterial chemotaxis
    • 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•].
    • (1996) J Biol Chem , vol.271 , pp. 17966-17973
    • Surette, M.G.1    Stock, J.B.2
  • 21
    • 0029803848 scopus 로고    scopus 로고
    • Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer
    • 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••].
    • (1996) Science , vol.274 , pp. 423-425
    • Tatsuno, I.1    Homma, M.2    Oosawa, K.3    Kawagishi, I.4
  • 22
    • 0029851704 scopus 로고    scopus 로고
    • Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain
    • 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.
    • (1996) Science , vol.274 , pp. 425-426
    • Gardina, P.J.1    Manson, M.D.2
  • 23
    • 0030775629 scopus 로고    scopus 로고
    • Probing the structure of the cytoplasmic domain of the aspartate receptor by targeted disulfide cross-linking
    • 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.
    • (1997) Biochemistry , vol.36 , pp. 11858-11864
    • Chen, X.1    Koshland D.E., Jr.2
  • 24
    • 0030811371 scopus 로고    scopus 로고
    • Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli
    • Park H, Inouye M: Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli. J Bacteriol 1997, 179:4382-4390.
    • (1997) J Bacteriol , vol.179 , pp. 4382-4390
    • Park, H.1    Inouye, M.2
  • 25
    • 0029779670 scopus 로고    scopus 로고
    • Mutational analysis of a transmembrane segment in a bacterial chemoreceptor
    • Baumgartner JW, Hazelbauer GL: Mutational analysis of a transmembrane segment in a bacterial chemoreceptor. J Bacteriol 1996, 178:4651-4660.
    • (1996) J Bacteriol , vol.178 , pp. 4651-4660
    • Baumgartner, J.W.1    Hazelbauer, G.L.2
  • 26
    • 0029910912 scopus 로고    scopus 로고
    • Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo
    • 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.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11546-11551
    • Hughson, A.G.1    Hazelbauer, G.L.2
  • 27
    • 0029865503 scopus 로고    scopus 로고
    • Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
    • Chervitz SA, Falke JJ: Molecular mechanism of transmembrane signaling by the aspartate receptor: A model. Proc Natl Acad Sci USA 1996, 93:2545-2550.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2545-2550
    • Chervitz, S.A.1    Falke, J.J.2
  • 28
    • 0030773005 scopus 로고    scopus 로고
    • Converting a transmembrane receptor to a soluble receptor: Recognition domain to effector domain signaling after excision of the transmembrane domain
    • 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.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11201-11204
    • Ottemann, K.M.1    Koshland D.E., Jr.2
  • 29
    • 0029979271 scopus 로고    scopus 로고
    • The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation
    • 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.
    • (1996) Biochemistry , vol.35 , pp. 4984-4993
    • Wu, J.1    Li, J.2    Li, G.3    Long, D.G.4    Weis, R.M.5
  • 30
    • 0030768758 scopus 로고    scopus 로고
    • The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process
    • Li J, Li G, Weis RM: The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process. Biochemistry 1997, 36:11851-11857.
    • (1997) Biochemistry , vol.36 , pp. 11851-11857
    • Li, J.1    Li, G.2    Weis, R.M.3
  • 31
    • 0030736078 scopus 로고    scopus 로고
    • Methylation of the Escherichia coli chemotaxis receptors: Intra- and interdimer mechanisms
    • Le Moual H, Quang T, Koshland DE Jr.: Methylation of the Escherichia coli chemotaxis receptors: intra- and interdimer mechanisms. Biochemistry 1997, 36:13441-13448.
    • (1997) Biochemistry , vol.36 , pp. 13441-13448
    • Le Moual, H.1    Quang, T.2    Koshland D.E., Jr.3
  • 32
    • 0031569882 scopus 로고    scopus 로고
    • Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine
    • 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.
    • (1997) Structure , vol.5 , pp. 545-558
    • Djordjevic, S.1    Stock, A.M.2
  • 33
    • 0030595328 scopus 로고    scopus 로고
    • Signal transduction via the multi-step phosphorelay: Not necessarily a road less traveled
    • Appleby JL, Parkinson JS, Bourret RB: Signal transduction via the multi-step phosphorelay: not necessarily a road less traveled. Cell 1996, 86:845-848.
    • (1996) Cell , vol.86 , pp. 845-848
    • Appleby, J.L.1    Parkinson, J.S.2    Bourret, R.B.3
  • 34
    • 0030984442 scopus 로고    scopus 로고
    • In vitro phosphorylation of the Arc two-component signal transduction system of Escherichia coli
    • 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.
    • (1997) J Bacteriol , vol.179 , pp. 5429-5435
    • Georgellis, D.1    Lynch, A.S.2    Lin, E.C.C.3
  • 35
    • 0029871035 scopus 로고    scopus 로고
    • Integration of multiple domains in a two-component sensor protein - The Bordetella pertussis BvgAS phosphorelay
    • 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.
    • (1996) EMBO J , vol.15 , pp. 1028-1036
    • Uhl, M.A.1    Miller, J.F.2
  • 36
    • 0030466066 scopus 로고    scopus 로고
    • Central role of the BvgS receiver as a phosphorylated intermediate in a complex two-component phosphorelay
    • 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.
    • (1996) J Biol Chem , vol.271 , pp. 33176-33180
    • Uhl, M.A.1    Miller, J.F.2
  • 37
    • 0029941952 scopus 로고    scopus 로고
    • An unorthodox sensor protein (TorS) mediates induction of the for structural genes in response to trimethylamine N-oxide in Escherichia coli
    • 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.
    • (1996) Mol Microbiol , vol.20 , pp. 1297-1306
    • Jourlin, C.1    Bengrine, A.2    Chippaux, M.3    Mejean, V.4
  • 38
    • 0031564650 scopus 로고    scopus 로고
    • Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli
    • 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.
    • (1997) J Mol Biol , vol.267 , pp. 770-777
    • Jourlin, C.1    Ansaldi, M.2    Mejean, V.3
  • 39
    • 0030912553 scopus 로고    scopus 로고
    • New classes of mutants in complementary chromatic adaptation provide evidence for a novel four-step phosphorelay system
    • 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.
    • (1997) J Bacteriol , vol.179 , pp. 3914-3921
    • Kehoe, D.M.1    Grossman, A.R.2
  • 40
    • 0030043573 scopus 로고    scopus 로고
    • Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker
    • 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.
    • (1996) Biochemistry , vol.35 , pp. 433-443
    • Zhou, H.1    McEvoy, M.M.2    Lowry, D.F.3    Swanson, R.V.4    Simon, Ml.5    Dahlquist, F.W.6
  • 41
    • 0031047030 scopus 로고    scopus 로고
    • Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR
    • Zhou H, Dahlquist FW: Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR. Biochemistry 1997, 36:699-710.
    • (1997) Biochemistry , vol.36 , pp. 699-710
    • Zhou, H.1    Dahlquist, F.W.2
  • 42
    • 0030940479 scopus 로고    scopus 로고
    • Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB
    • 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.
    • (1997) Cell , vol.88 , pp. 717-723
    • Kato, M.1    Mizuno, T.2    Shimizu, T.3    Hakoshima, T.4
  • 43
    • 0029931125 scopus 로고    scopus 로고
    • Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy
    • 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.
    • (1996) Biochemistry , vol.35 , pp. 5633-5640
    • McEvoy, M.M.1    Muhandiram, D.R.2    Kay, L.E.3    Dahlquist, F.W.4
  • 44
    • 0031038354 scopus 로고    scopus 로고
    • A bacterial basic region leucine zipper histidine kinase regulating toluene degradation
    • Lau PCK, Wang Y, Patel A, Labbe D, Bergeron H, Brousseau R, Konishi Y, Rawlings M: A bacterial basic region leucine zipper histidine kinase regulating toluene degradation. Proc Natl Acad Sci USA 1997, 94:1453-1458. This paper contains the first report of a bacterial two-component system, TodST, involved in aromatic hydrocarbon metabolic regulation. The todS gene encodes a hybrid sensory kinase with a leucine zipper dimerization motif. The todS gene is also unusual in that it contains two separate histidine kinase domains and a putative oxygen-sensing heme-containing domain. The authors speculate that TodS is possibly a 'dual sensor' capable of responding to changes in environmental toluene levels and to sensing oxidative stress.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1453-1458
    • Lau, P.C.K.1    Wang, Y.2    Patel, A.3    Labbe, D.4    Bergeron, H.5    Brousseau, R.6    Konishi, Y.7    Rawlings, M.8
  • 45
    • 0030068603 scopus 로고    scopus 로고
    • Dimerization is required for the activity of the protein histidine kinase CheA that mediates signal transduction in bacterial chemotaxis
    • Surette MG, Levit M, Liu Y, Lukat G, Ninfa EG, Ninfa A, Stock JB: Dimerization is required for the activity of the protein histidine kinase CheA that mediates signal transduction in bacterial chemotaxis. J Biol Chem 1996, 271:939-945.
    • (1996) J Biol Chem , vol.271 , pp. 939-945
    • Surette, M.G.1    Levit, M.2    Liu, Y.3    Lukat, G.4    Ninfa, E.G.5    Ninfa, A.6    Stock, J.B.7
  • 46
    • 0029731415 scopus 로고    scopus 로고
    • Active site interference and asymmetric activation in the chemotaxis protein histidine kinase CheA
    • Levit M, Liu Y, Surette M, Stock J: Active site interference and asymmetric activation in the chemotaxis protein histidine kinase CheA. J Biol Chem 1996, 271:32057-32063,
    • (1996) J Biol Chem , vol.271 , pp. 32057-32063
    • Levit, M.1    Liu, Y.2    Surette, M.3    Stock, J.4
  • 47
    • 0031037310 scopus 로고    scopus 로고
    • Genetic analysis of the catalytic domain of the chemotaxis-associated histidine kinase CheA
    • Ellefson DD, Weber U, Wolfe AJ: Genetic analysis of the catalytic domain of the chemotaxis-associated histidine kinase CheA. J Bacteriol 1997, 179:825-830.
    • (1997) J Bacteriol , vol.179 , pp. 825-830
    • Ellefson, D.D.1    Weber, U.2    Wolfe, A.J.3
  • 48
    • 0030585421 scopus 로고    scopus 로고
    • Crystal structure of a phosphatase-resistant mutant of sporulation response regulator SpoOf from Bacillus subtilis
    • Madhusudan, Zapf J, Whiteley JM, Hoch JA, Xuong NH, Varughese Kl: Crystal structure of a phosphatase-resistant mutant of sporulation response regulator SpoOF from Bacillus subtilis. Structure 1996, 4:679-690. These two papers [48•,49•] describe independent structural determinations of SpoOF, the B. subtilis sporulation response regulator which is structurally homologous to CheY. This group reports the X-ray crystallographic structural solution of a single-site mutant of SpoOF that is Rap phosphatase-resistant, while the other group reports an NMR-derived structure of the wild-type protein [49•]. Both groups determine that SpoOF has the same doubly-wound five-stranded α/ß fold of CheY.
    • (1996) Structure , vol.4 , pp. 679-690
    • Madhusudan1    Zapf, J.2    Whiteley, J.M.3    Hoch, J.A.4    Xuong, N.H.5    Varughese, Kl.6
  • 49
    • 0030850026 scopus 로고    scopus 로고
    • High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, SpoOF: Implications for phosphorylation and molecular recognition
    • Feher VA, Zapf JW, Hoch JA, Whiteley JM, McIntosh LP, Rance M, Skelton NJ, Dahlquist FW, Cavanagh J: High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, SpoOF: Implications for phosphorylation and molecular recognition. Biochemistry 1997, 36:10015-10025. See annotation [48•].
    • (1997) Biochemistry , vol.36 , pp. 10015-10025
    • Feher, V.A.1    Zapf, J.W.2    Hoch, J.A.3    Whiteley, J.M.4    McIntosh, L.P.5    Rance, M.6    Skelton, N.J.7    Dahlquist, F.W.8    Cavanagh, J.9
  • 50
    • 0028927334 scopus 로고
    • Three-dimensional solution structure of the N-terminal receiver domain of NTRC
    • Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE: Three-dimensional solution structure of the N-terminal receiver domain of NTRC. Biochemistry 1995, 34:1413-1424.
    • (1995) Biochemistry , vol.34 , pp. 1413-1424
    • Volkman, B.F.1    Nohaile, M.J.2    Amy, N.K.3    Kustu, S.4    Wemmer, D.E.5
  • 51
    • 0029736725 scopus 로고    scopus 로고
    • Structure of the Escherichia coli response regulator NarL
    • Baikalov I, Schrsder I, Kaczor-Grzeskowiak M, Grzeskowiak K, Gunsalus RP, Dickerson RE: Structure of the Escherichia coli response regulator NarL. Biochemistry 1996, 35:11053-11061. This paper contains the first report of the structure of a multidomain response regulator, NarL of the nitrate-sensing system, NarL is a representative of the FixJ/LuxR subfamily of response regulators involved in transcriptional activation. This structure yields the first direct evidence of a possible mechanism for inhibition of effector domain activity by the regulatory domain. The amino-terminal regulatory domain blocks the access of the carboxy-terminal helix-turn-helix DNA-binding motif to its target DNA sequence.
    • (1996) Biochemistry , vol.35 , pp. 11053-11061
    • Baikalov, I.1    Schrsder, I.2    Kaczor-Grzeskowiak, M.3    Grzeskowiak, K.4    Gunsalus, R.P.5    Dickerson, R.E.6
  • 52
    • 0032539671 scopus 로고    scopus 로고
    • Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain
    • in press
    • Djordjevic S, Goudreau PN, Xu Q, Stock AM, West AH: Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Proc Natl Acad Sci USA 1998, in press. These authors report the structure of a multidomain response regulator with a well-ordered linker, the bacterial chemotaxis regulator CheB in its unphospharylated form. CheB is representative of the third major subfamily of re sponse regulators, those which are not involved in transcriptional activation. The amino-terminal regulatory domain packs up against the carboxy-terminal methylesterase domain, thereby blocking access of the active site to substrate chemoreceptors. The authors compare the structure of CheB to that of NarL and propose a general mechanism for phosphorylation-triggered activation of multidomain response regulators.
    • (1998) Proc Natl Acad Sci USA
    • Djordjevic, S.1    Goudreau, P.N.2    Xu, Q.3    Stock, A.M.4    West, A.H.5
  • 53
    • 0031952431 scopus 로고    scopus 로고
    • Crystal Structures of CheY from Thermotoga maritim a do not support conventional explanations for the structural basis of enhanced thermostability
    • in press
    • Usher KC, de la Cruz AF, Dahlquist FW, Swanson RV, Simon Ml, Remington SJ: Crystal Structures of CheY from Thermotoga maritim a do not support conventional explanations for the structural basis of enhanced thermostability. Protein Sci 1998, in press.
    • (1998) Protein Sci
    • Usher, K.C.1    De La Cruz, A.F.2    Dahlquist, F.W.3    Swanson, R.V.4    Simon, Ml.5    Remington, S.J.6
  • 54
    • 0031007417 scopus 로고    scopus 로고
    • Uncoupled phosphorylation and activation in bacterial chemotaxis: The 2.3 Ȧ structure of an aspartate to lysine mutant at position 13 of CheY
    • Jiang M, Bourret RB, Simon Ml, Volz K: Uncoupled phosphorylation and activation in bacterial chemotaxis: The 2.3 Ȧ structure of an aspartate to lysine mutant at position 13 of CheY. J Biol Chem 1997, 272:11850-11855.
    • (1997) J Biol Chem , vol.272 , pp. 11850-11855
    • Jiang, M.1    Bourret, R.B.2    Simon, Ml.3    Volz, K.4
  • 55
    • 0029863506 scopus 로고    scopus 로고
    • The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism
    • Bellsolell L, Cronet P, Majolero M, Serrano L, Coll M: The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism. J Mol Biol 1996, 257:116-128.
    • (1996) J Mol Biol , vol.257 , pp. 116-128
    • Bellsolell, L.1    Cronet, P.2    Majolero, M.3    Serrano, L.4    Coll, M.5
  • 56
    • 0031058440 scopus 로고    scopus 로고
    • Crystal structures of CheY mutants Y106W and T871/Y106W: CheY activation correlates with movement of residue 106
    • Zhu X, Rebello J, Matsumura P, Volz K: Crystal structures of CheY mutants Y106W and T871/Y106W: CheY activation correlates with movement of residue 106. J Biol Chem 1997, 272:5000-5006. The structures of two single-site mutants (T871, Y106W) and of the corresponding double-site mutant (T871/Y106W) of E. coli CheY shed light on the role of residue Y106 in phosphorylation-dependent activation of CheY activity. The signaling ability of CheY is modulated by movement of the phenolic side chain of Y106 between 'inside1 and 'outside' positions within the context of the CheY structure.
    • (1997) J Biol Chem , vol.272 , pp. 5000-5006
    • Zhu, X.1    Rebello, J.2    Matsumura, P.3    Volz, K.4
  • 57
    • 0029900040 scopus 로고    scopus 로고
    • Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichis coli
    • Zhu X, Amsler CD, Volz K, Matsumura P: Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichis coli. J Bacteriol 1996, 178:4208-4215.
    • (1996) J Bacteriol , vol.178 , pp. 4208-4215
    • Zhu, X.1    Amsler, C.D.2    Volz, K.3    Matsumura, P.4
  • 58
    • 0031568318 scopus 로고    scopus 로고
    • The DNA-binding domain of OmpR: Crystal structure of a winged-helix transcription factor
    • Martinez-Hackert E, Stock AM: The DNA-binding domain of OmpR: crystal structure of a winged-helix transcription factor. Structure 1997, 5:109-124. These papers [58•,59•] report independent solutions for the structure of the carboxy-terminal DNA-binding domain of OmpR the E. coli osmolarity-dependent response regulator. OmpR is representative of a family of DNA-binding proteins termed 'winged-helix-turn-helix' proteins. These reports provide the first structural information for the OmpR/PhoB subfamily of bacterial response regulators involved in transcriptional activation.
    • (1997) Structure , vol.5 , pp. 109-124
    • Martinez-Hackert, E.1    Stock, A.M.2
  • 59
    • 0031027087 scopus 로고    scopus 로고
    • Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site
    • Kondo H, Nakagawa A, Nishihira J, Nishimura Y, Mizuno T, Tanaka I: Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site. Nat Struct Biol 1997, 4:28-31. See annotation [58•].
    • (1997) Nat Struct Biol , vol.4 , pp. 28-31
    • Kondo, H.1    Nakagawa, A.2    Nishihira, J.3    Nishimura, Y.4    Mizuno, T.5    Tanaka, I.6
  • 60
    • 0031566431 scopus 로고    scopus 로고
    • Structural relationships in the OmpR family of winged-helix transcription factors
    • Martinez-Hackert E, Stock AM: Structural relationships in the OmpR family of winged-helix transcription factors. J Mol Biol 1997, 269:301-312.
    • (1997) J Mol Biol , vol.269 , pp. 301-312
    • Martinez-Hackert, E.1    Stock, A.M.2
  • 61
    • 0029164694 scopus 로고
    • A common switch in activation of the response regulators NtrC and PhoB: Phosphorylation induces dimerization of the receiver modules
    • Fiedler U, Weiss V: A common switch in activation of the response regulators NtrC and PhoB: phosphorylation induces dimerization of the receiver modules. EMBO J 1995, 14:3696-3705,
    • (1995) EMBO J , vol.14 , pp. 3696-3705
    • Fiedler, U.1    Weiss, V.2
  • 62
    • 0030580087 scopus 로고    scopus 로고
    • Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR
    • Huang K-J, Igo MM: Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR. J Mol Biol 1996, 262:615-628.
    • (1996) J Mol Biol , vol.262 , pp. 615-628
    • Huang, K.-J.1    Igo, M.M.2
  • 63
    • 0030940341 scopus 로고    scopus 로고
    • Phosphorylation stimulates the cooperative DNA-binding properties of the transcription factor OmpR
    • Huang K-E, Lan C-Y, Igo MM: Phosphorylation stimulates the cooperative DNA-binding properties of the transcription factor OmpR. Proc Natl Acad Sci USA 1997, 94:2828-2832.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2828-2832
    • Huang, K.-E.1    Lan, C.-Y.2    Igo, M.M.3
  • 64
    • 0030797034 scopus 로고    scopus 로고
    • Involvement of the amino-terminal phosphorylation module of UhpA in activation of uhpT transcription in Escherichia coli
    • Webber CA, Kadner RJ: Involvement of the amino-terminal phosphorylation module of UhpA in activation of uhpT transcription in Escherichia coli. Mol Microbiol 1997, 24:1039 1048.
    • (1997) Mol Microbiol , vol.24 , pp. 10391048
    • Webber, C.A.1    Kadner, R.J.2
  • 65
    • 0030894489 scopus 로고    scopus 로고
    • Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein
    • Wyman C, Rombel I, North AK, Bustamente C, Kustu S: Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein. Science 1997, 275:1658-1661. Report of a study in which scanning force microscopy was used to visualize large oligomers of NtrC, the bacterial enhancer-binding protein. Phosphorylation triggered the formation of even larger complexes. The authors then went on to show that these large complexes of phospho NtrC are required for transcriptional activation of the σ54-holoenzyme.
    • (1997) Science , vol.275 , pp. 1658-1661
    • Wyman, C.1    Rombel, I.2    North, A.K.3    Bustamente, C.4    Kustu, S.5
  • 66
    • 0030873934 scopus 로고    scopus 로고
    • The CheZ-binding surface of CheY overlaps the CheA- and FliM-binding surfaces
    • Zhu X, Volz K, Matsumura P: The CheZ-binding surface of CheY overlaps the CheA- and FliM-binding surfaces. J Biol Chem 1997, 272:23753-23764. This sludy reports the characterization of CheY mutants exhibiting altered CheZ-binding abilities. The authors identify a CheY surface involved in CheZ-binding and then go on to map and compare this surface to the previously identified surfaces implicated in CheA and FIiM binding. They conclude that these three proteins bind to surfaces on CheY that overlap, but that the surfaces are not completely identical.
    • (1997) J Biol Chem , vol.272 , pp. 23753-23764
    • Zhu, X.1    Volz, K.2    Matsumura, P.3
  • 67
    • 0029988249 scopus 로고    scopus 로고
    • Altered recognition mutants of the response regulator PhoB: A new genetic strategy for studying protein-protein interactions
    • Haldimann A, Prahalad MK, Fisher SL, Kim S-K, Walsh CT, Wanner BL: Altered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions. Proc Natl Acad Sci USA 1996, 93:14361 14366.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1436114366
    • Haldimann, A.1    Prahalad, M.K.2    Fisher, S.L.3    Kim, S.-K.4    Walsh, C.T.5    Wanner, B.L.6
  • 68
    • 0030813090 scopus 로고    scopus 로고
    • Molecular recognition in signal transduction: The interaction surfaces of the SpoOf response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis
    • Tzeng Y-L, Hoch JA: Molecular recognition in signal transduction: the interaction surfaces of the SpoOF response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis. J Mol Biol 1997, 272:200-212.
    • (1997) J Mol Biol , vol.272 , pp. 200-212
    • Tzeng, Y.-L.1    Hoch, J.A.2
  • 69
    • 0031576335 scopus 로고    scopus 로고
    • Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface
    • Nohaile M, Kern D, Wemmer D, Stedman K, Kustu S: Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: evidence for an activating surface. J Mol Biol 1997, 273:299-316.
    • (1997) J Mol Biol , vol.273 , pp. 299-316
    • Nohaile, M.1    Kern, D.2    Wemmer, D.3    Stedman, K.4    Kustu, S.5
  • 70
    • 0029743605 scopus 로고    scopus 로고
    • Fancy meeting you herel A fresh look at "prokaryotic* protein phosphorylation
    • Kennelly PJ, Potts M: Fancy meeting you herel A fresh look at "prokaryotic* protein phosphorylation. J Bacteriol 1996, 178:4759-4764.
    • (1996) J Bacteriol , vol.178 , pp. 4759-4764
    • Kennelly, P.J.1    Potts, M.2
  • 71
    • 0029915601 scopus 로고    scopus 로고
    • Bacterial signalling involving eucaryotic-type protein kinases
    • Zhang C-C: Bacterial signalling involving eucaryotic-type protein kinases. Mol Microbiol 1996, 20:9-15
    • (1996) Mol Microbiol , vol.20 , pp. 9-15
    • Zhang, C.-C.1
  • 72
    • 0031016266 scopus 로고    scopus 로고
    • Pkn9, a Ser/Thr protein kinase involved in the development of Myxococcus xanthus
    • Hanlon WA, Inouye M, Inouye S: Pkn9, a Ser/Thr protein kinase involved in the development of Myxococcus xanthus. Mol Microbiol 1997, 23:459-471.
    • (1997) Mol Microbiol , vol.23 , pp. 459-471
    • Hanlon, W.A.1    Inouye, M.2    Inouye, S.3
  • 73
    • 0029903729 scopus 로고    scopus 로고
    • Effects of overproduction of Pkn2, a transmembrane protein serine/threonine kinase, on development of Myxococcus xanthus
    • Udo H, Inouye M, Inouye S: Effects of overproduction of Pkn2, a transmembrane protein serine/threonine kinase, on development of Myxococcus xanthus. J Bacteriol 1996, 178:6647-6649.
    • (1996) J Bacteriol , vol.178 , pp. 6647-6649
    • Udo, H.1    Inouye, M.2    Inouye, S.3
  • 74
    • 0029971544 scopus 로고    scopus 로고
    • Reciprocal regulation of the differentiation of Myxococcus xanthus by Pkn5 and Pkn6, eukaryotic-like Ser/Thr protein kinases
    • Zhang W, Inouye M, Inouye S: Reciprocal regulation of the differentiation of Myxococcus xanthus by Pkn5 and Pkn6, eukaryotic-like Ser/Thr protein kinases. Mol Microbiol 1996, 20:435-447.
    • (1996) Mol Microbiol , vol.20 , pp. 435-447
    • Zhang, W.1    Inouye, M.2    Inouye, S.3
  • 75
    • 0030009174 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in Myxococcus xanthus, a multicellular prokaryote
    • Frasch SC, Dworkin M: Tyrosine phosphorylation in Myxococcus xanthus, a multicellular prokaryote. J Bacteriol 1996, 178:4084 4088.
    • (1996) J Bacteriol , vol.178 , pp. 40844088
    • Frasch, S.C.1    Dworkin, M.2
  • 76
    • 0030938650 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation in the cyanobacterium Anabaena sp. strain PCC 7120
    • McCartney B, Howell LD, Kennelly PJ. Potts M: Protein tyrosine phosphorylation in the cyanobacterium Anabaena sp. strain PCC 7120. J Bacteriol 1997, 179:2314-231B.
    • (1997) J Bacteriol , vol.179
    • McCartney, B.1    Howell, L.D.2    Kennelly, P.J.3    Potts, M.4
  • 77
    • 0030886811 scopus 로고    scopus 로고
    • Properties of the phosphorylation reaction catalyzed by SpollAB that help to regulate sporulation of Bacillus subtilis
    • Najafi SMA, Harris DA, Yudkin MD: Properties of the phosphorylation reaction catalyzed by SpollAB that help to regulate sporulation of Bacillus subtilis. J Bacteriol 1997, 179:5628-5631.
    • (1997) J Bacteriol , vol.179 , pp. 5628-5631
    • Najafi, S.M.A.1    Harris, D.A.2    Yudkin, M.D.3
  • 78
    • 0031014176 scopus 로고    scopus 로고
    • Structural relationship between a bacterial developmental protein and eukaryotic PP2C protein phosphatases
    • Adler E, Donella-Deana A, Arigoni F, Pinna LA, Stragier P: Structural relationship between a bacterial developmental protein and eukaryotic PP2C protein phosphatases. Mol Microbiol 1997, 23:57-62.
    • (1997) Mol Microbiol , vol.23 , pp. 57-62
    • Adler, E.1    Donella-Deana, A.2    Arigoni, F.3    Pinna, L.A.4    Stragier, P.5
  • 79
    • 8244259184 scopus 로고    scopus 로고
    • Modulator protein RsbR regulates environmental signalling in the general stress pathway of Bacillus subtilis
    • Akbar S, Kang CM, Gaidenko TA, Price CW: Modulator protein RsbR regulates environmental signalling in the general stress pathway of Bacillus subtilis. Mol Microbiol 1997, 24:567-578.
    • (1997) Mol Microbiol , vol.24 , pp. 567-578
    • Akbar, S.1    Kang, C.M.2    Gaidenko, T.A.3    Price, C.W.4
  • 80
    • 0030002810 scopus 로고    scopus 로고
    • A deduced Thermomonospora curvata protein containing serine/threonine protein kinase and WD-repeat domains
    • Janda L, Tichy P, Spizek J, Petricek M: A deduced Thermomonospora curvata protein containing serine/threonine protein kinase and WD-repeat domains. J Bacteriol 1996, 178:1487-1489.
    • (1996) J Bacteriol , vol.178 , pp. 1487-1489
    • Janda, L.1    Tichy, P.2    Spizek, J.3    Petricek, M.4
  • 81
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7
    • Volz K, Matsumura P: Crystal structure of Escherichia coli CheY refined at 1.7 Ȧ resolution. J Biol Chem 1991, 266:15511-15519.
    • (1991) Ȧ Resolution. J Biol Chem , vol.266 , pp. 15511-15519
    • Volz, K.1    Matsumura, P.2


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