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Volumn 86, Issue 2, 1996, Pages 331-339

ATP binding to the σ54-dependent activator XylR triggers a protein multimerization cycle catalyzed by UAS DNA

Author keywords

[No Author keywords available]

Indexed keywords

DNA; RNA POLYMERASE;

EID: 0030602821     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80104-X     Document Type: Article
Times cited : (78)

References (55)
  • 1
    • 0026501223 scopus 로고
    • Unscrambling the puzzle of biological machines: The importance of the details
    • Alberts, B., and Miake-Lye, R. (1992). Unscrambling the puzzle of biological machines: the importance of the details. Cell 68, 415-420.
    • (1992) Cell , vol.68 , pp. 415-420
    • Alberts, B.1    Miake-Lye, R.2
  • 2
    • 0026581288 scopus 로고
    • The prokaryotic enhancer binding protein NtrC has an ATPase activity which is phosphorylation and DNA dependent
    • Austin, S., and Dixon, R. (1992). The prokaryotic enhancer binding protein NtrC has an ATPase activity which is phosphorylation and DNA dependent. EMBO J. 11, 2219-2228.
    • (1992) EMBO J. , vol.11 , pp. 2219-2228
    • Austin, S.1    Dixon, R.2
  • 3
    • 0028363001 scopus 로고
    • Purification and in vitro activity of a truncated form of AnfA, transcriptional activator protein of alternative nitrogenase from Azotobacter vinelandii
    • Austin, S., and Lambert, J. (1994). Purification and in vitro activity of a truncated form of AnfA, transcriptional activator protein of alternative nitrogenase from Azotobacter vinelandii. J. Biol. Chem. 269, 18141-18148.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18141-18148
    • Austin, S.1    Lambert, J.2
  • 4
    • 0025058956 scopus 로고
    • Characterization of theKlebsiella pneumonias nitrogen-fixation regulatory proteins NifA and NifL in vitro
    • Austin, S., Henderson, N., and Dixon, R. (1990). Characterization of theKlebsiella pneumonias nitrogen-fixation regulatory proteins NifA and NifL in vitro. Eur. J. Biochem. 187, 353-360.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 353-360
    • Austin, S.1    Henderson, N.2    Dixon, R.3
  • 5
    • 0027958569 scopus 로고
    • The isolated catalytic domain of NifA, a bacterial enhancer-binding protein, activates transcription in vitro: Activation is inhibited by NifL
    • Berger, D.K., Narberhaus, F., and Kustu, S. (1994). The isolated catalytic domain of NifA, a bacterial enhancer-binding protein, activates transcription in vitro: activation is inhibited by NifL. Proc. Natl. Acad. Sci. USA 91, 103-107.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 103-107
    • Berger, D.K.1    Narberhaus, F.2    Kustu, S.3
  • 6
    • 0026026818 scopus 로고
    • The GTPase super-family: Conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, D.A., and McCormick, F. (1991). The GTPase super-family: conserved structure and molecular mechanism. Nature 349, 117-127
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 7
    • 0025971243 scopus 로고
    • Role of integration host factor in the regulation of the glnHp2 promoter of Escherichia coli
    • Claverie-Martin, F., and Magasanik, B. (1991). Role of integration host factor in the regulation of the glnHp2 promoter of Escherichia coli. Proc. Natl. Acad. Sci. USA 88, 1631-1635.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1631-1635
    • Claverie-Martin, F.1    Magasanik, B.2
  • 9
    • 0028244041 scopus 로고
    • Genetic evidence for activation of the positive transcriptional regulator XylR, a member of the NtrC family of regulators, by effector binding
    • Delgado, A., and Ramos, J.L. (1994). Genetic evidence for activation of the positive transcriptional regulator XylR, a member of the NtrC family of regulators, by effector binding. J. Biol. Chem. 269, 8059-8062.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8059-8062
    • Delgado, A.1    Ramos, J.L.2
  • 11
    • 0029063837 scopus 로고
    • Activation of the transcriptional regulator XylR of Pseudomonas putida by release of repression between functional domains
    • Fernández, S., de Lorenzo, V., and Pérez-Martín, J. (1995). Activation of the transcriptional regulator XylR of Pseudomonas putida by release of repression between functional domains. Mol. Microbiol. 16, 205-213.
    • (1995) Mol. Microbiol. , vol.16 , pp. 205-213
    • Fernández, S.1    De Lorenzo, V.2    Pérez-Martín, J.3
  • 12
    • 0029016807 scopus 로고
    • Constitutive forms of the enhancer-binding protein NtrC: Evidence that essential oligomerization determinants lie in the central activation domain
    • Flashner, Y., Weiss, D.S., Keener, J., and Kustu, S. (1995). Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain. J. Mol. Biol. 249, 700-713.
    • (1995) J. Mol. Biol. , vol.249 , pp. 700-713
    • Flashner, Y.1    Weiss, D.S.2    Keener, J.3    Kustu, S.4
  • 13
    • 0025171151 scopus 로고
    • Integration host factor is required for the activation of developmentally regulated genes in Caulobacter
    • Gober, J.W., and Shapiro, L. (1990). Integration host factor is required for the activation of developmentally regulated genes in Caulobacter. Genes Dev. 4, 1494-1504.
    • (1990) Genes Dev. , vol.4 , pp. 1494-1504
    • Gober, J.W.1    Shapiro, L.2
  • 14
    • 0028286432 scopus 로고
    • 54-dependent transcriptional activator, may be negatively controlled by a subdomain in the C-terminal end of its two-component receiver module
    • 54-dependent transcriptional activator, may be negatively controlled by a subdomain in the C-terminal end of its two-component receiver module. Mol. Microbiol. 13, 51-66.
    • (1994) Mol. Microbiol. , vol.13 , pp. 51-66
    • Gu, B.1    Lee, J.H.2    Hoover, T.R.3    Scholl, D.4    Nixon, B.T.5
  • 15
    • 0027965030 scopus 로고
    • Regulated expression in vitro of genes coding for formate hydrogenolyase components of Escherichia coli
    • Hooper, S., Babst, M., Schlensog, V., Fischer, H.M., Hennecke, H., and Bock, A. (1994). Regulated expression in vitro of genes coding for formate hydrogenolyase components of Escherichia coli. J. Biol. Chem. 269, 19597-19604.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19597-19604
    • Hooper, S.1    Babst, M.2    Schlensog, V.3    Fischer, H.M.4    Hennecke, H.5    Bock, A.6
  • 16
    • 0029044907 scopus 로고
    • 54-dependent transcriptional activator FhlA from Escherichia coli
    • 54-dependent transcriptional activator FhlA from Escherichia coli. J. Bacteriol. 177, 2798-2803.
    • (1995) J. Bacteriol. , vol.177 , pp. 2798-2803
    • Hooper, S.1    Böck, A.2
  • 17
    • 0025012093 scopus 로고
    • Integration host factor stimulates interaction of RNA polymerase with NifA, the transcriptional activator for nitrogen fixation operons
    • Hoover, T.R., Santero, E., Porter, S., and Kustu, S. (1990). Integration host factor stimulates interaction of RNA polymerase with NifA, the transcriptional activator for nitrogen fixation operons. Cell 63, 11-22.
    • (1990) Cell , vol.63 , pp. 11-22
    • Hoover, T.R.1    Santero, E.2    Porter, S.3    Kustu, S.4
  • 18
    • 0026532670 scopus 로고
    • The central domain of Rhizobium leguminosarum DctD functions independently to activate transcription
    • Huala, E., Stigter, J., and Ausubel, F.M. (1992). The central domain of Rhizobium leguminosarum DctD functions independently to activate transcription. J. Bacteriol. 174, 1428-1431.
    • (1992) J. Bacteriol. , vol.174 , pp. 1428-1431
    • Huala, E.1    Stigter, J.2    Ausubel, F.M.3
  • 19
    • 0024040412 scopus 로고
    • Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: Roles of the conserved amino-terminal domain of NTRC
    • Keener, J., and Kustu, S. (1988). Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: roles of the conserved amino-terminal domain of NTRC. Proc. Natl. Acad. Sci. USA 85, 4976-4980.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4976-4980
    • Keener, J.1    Kustu, S.2
  • 20
    • 0028012039 scopus 로고
    • Different agonist-and antagonist-induced conformational changes in retinoic acid receptors analysed by protease mapping
    • Keidel, S., LeMotte, P., and Apfel, C. (1994). Different agonist-and antagonist-induced conformational changes in retinoic acid receptors analysed by protease mapping. Mol. Cell. Biol. 14, 287-298.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 287-298
    • Keidel, S.1    Lemotte, P.2    Apfel, C.3
  • 21
    • 0027162310 scopus 로고
    • Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein
    • Klose, K.E., Weiss, D.S., and Kustu, S. (1993). Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein. J. Mol. Biol. 232, 67-78.
    • (1993) J. Mol. Biol. , vol.232 , pp. 67-78
    • Klose, K.E.1    Weiss, D.S.2    Kustu, S.3
  • 22
    • 0024728119 scopus 로고
    • Expression of sigma-54 (nfrA)-dependent genes is probably united by a common mechanism
    • Kustu, S., Santero, E., Keener, J., Popham, D., and Weiss, D. (1989). Expression of sigma-54 (nfrA)-dependent genes is probably united by a common mechanism. Microbiol. Rev. 53, 367-376.
    • (1989) Microbiol. Rev. , vol.53 , pp. 367-376
    • Kustu, S.1    Santero, E.2    Keener, J.3    Popham, D.4    Weiss, D.5
  • 23
    • 0025938894 scopus 로고
    • Prokaryotic transcriptional enhancers and enhancer-binding proteins
    • Kustu, S., North, A.K., and Weiss, D. (1991). Prokaryotic transcriptional enhancers and enhancer-binding proteins. Trends Biochem. Sci. 16, 397-402.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 397-402
    • Kustu, S.1    North, A.K.2    Weiss, D.3
  • 24
    • 0027468370 scopus 로고
    • Activity of purified NifA, a transcriptional activator of nitrogen fixation genes
    • Lee, H.S., Berger, D.K., and Kustu, S. (1993). Activity of purified NifA, a transcriptional activator of nitrogen fixation genes. Proc. Natl. Acad. Sci. USA 90, 2266-2270.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2266-2270
    • Lee, H.S.1    Berger, D.K.2    Kustu, S.3
  • 27
    • 0027282545 scopus 로고
    • Transcriptional control of the Pseudomonas putidaTOL plasmid catabolic pathways
    • Marqués, S., and Ramos, J.L. (1993). Transcriptional control of the Pseudomonas putidaTOL plasmid catabolic pathways. Mol. Microbiol. 9, 923-929.
    • (1993) Mol. Microbiol. , vol.9 , pp. 923-929
    • Marqués, S.1    Ramos, J.L.2
  • 28
    • 0018846636 scopus 로고
    • Sequencing end-labelled DNA with base-specific chemical cleavages
    • Maxam, A.M., and Gilbert, W. (1980). Sequencing end-labelled DNA with base-specific chemical cleavages. Meth. Enzymol. 65, 499-560.
    • (1980) Meth. Enzymol. , vol.65 , pp. 499-560
    • Maxam, A.M.1    Gilbert, W.2
  • 29
    • 0029148094 scopus 로고
    • Mechanism of activation of a response regulator: Interaction of NtrC-P dimers induces ATPase activity
    • Mettke, I., Fiedler, U., and Weiss, V. (1995). Mechanism of activation of a response regulator: interaction of NtrC-P dimers induces ATPase activity. J. Bacteriol. 177, 5056-5061.
    • (1995) J. Bacteriol. , vol.177 , pp. 5056-5061
    • Mettke, I.1    Fiedler, U.2    Weiss, V.3
  • 30
    • 0027340543 scopus 로고
    • 54-bacterial enhancer-binding protein family: Mechanism of action and phylogenetic relationship of their functional domains
    • 54-bacterial enhancer-binding protein family: mechanism of action and phylogenetic relationship of their functional domains. J. Bacteriol. 178, 6067-6074.
    • (1993) J. Bacteriol. , vol.178 , pp. 6067-6074
    • Morett, E.1    Segovia, L.2
  • 31
    • 0000451424 scopus 로고
    • Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli
    • Ninfa, A.J., and Magasanik, B. (1986). Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli. Proc. Natl. Acad. Sci. USA 83, 5909-5913.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5909-5913
    • Ninfa, A.J.1    Magasanik, B.2
  • 32
    • 0011559747 scopus 로고
    • Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and nfrC
    • Nixon, B.T., Ronson, C.W., and Ausubel, F.M. (1986). Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and nfrC. Proc. Natl. Acad. Sci. USA 83, 7850-7854.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7850-7854
    • Nixon, B.T.1    Ronson, C.W.2    Ausubel, F.M.3
  • 33
    • 0027248437 scopus 로고
    • Prokaryotic enhancer-binding proteins reflect eukaryotic-like modularity: The puzzle of nitrogen regulatory protein C
    • North, A.K., Klose, K.E., Stedman, M., and Kustu, S. (1993). Prokaryotic enhancer-binding proteins reflect eukaryotic-like modularity: the puzzle of nitrogen regulatory protein C. J. Bacteriol. 175, 4267-4273.
    • (1993) J. Bacteriol. , vol.175 , pp. 4267-4273
    • North, A.K.1    Klose, K.E.2    Stedman, M.3    Kustu, S.4
  • 34
    • 0028980296 scopus 로고
    • 54-dependent promoter Ps of the TOL plasmid of Pseudomonas putida requires HU for transcriptional activation in vivo by XylR
    • 54-dependent promoter Ps of the TOL plasmid of Pseudomonas putida requires HU for transcriptional activation in vivo by XylR. J. Bacteriol. 177, 3758-3763.
    • (1995) J. Bacteriol. , vol.177 , pp. 3758-3763
    • Pérez-Martín, J.1    De Lorenzo, V.2
  • 35
    • 0029073435 scopus 로고
    • The N-terminal domain of the prokaryotic enhancer-binding protein XylR is a specific intramolecular repressor
    • Pérez-Martín, J., and de Lorenzo, V. (1995b).The N-terminal domain of the prokaryotic enhancer-binding protein XylR is a specific intramolecular repressor. Proc. Natl. Acad. Sci. USA 92, 9392-9396.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9392-9396
    • Pérez-Martín, J.1    De Lorenzo, V.2
  • 36
    • 0029919623 scopus 로고    scopus 로고
    • 54-dependent transcriptional activator of Pseudomonas putida
    • 54-dependent transcriptional activator of Pseudomonas putida. J. Mol. Biol. 258, 575-587.
    • (1996) J. Mol. Biol. , vol.258 , pp. 575-587
    • Pérez-Martín, J.1    De Lorenzo, V.2
  • 38
    • 0028100756 scopus 로고
    • 54-dependent promoter Pu of the upper-TOL operon by intrinsically curved sequences
    • 54-dependent promoter Pu of the upper-TOL operon by intrinsically curved sequences. J. Biol. Chem. 269, 22657-22662.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22657-22662
    • Pérez-Martín, J.1    Timmis, K.N.2    De Lorenzo, V.3
  • 39
    • 0024598928 scopus 로고
    • Function of a bacterial activator protein that binds to transcriptional enhancers
    • Popham, D.L., Szeto, D., Keener, J., and Kustu, S. (1989). Function of a bacterial activator protein that binds to transcriptional enhancers. Science 243, 629-635.
    • (1989) Science , vol.243 , pp. 629-635
    • Popham, D.L.1    Szeto, D.2    Keener, J.3    Kustu, S.4
  • 40
    • 0027359777 scopus 로고
    • Oligomerization of NtrC at the glnA enhancer is required for transcriptional activation
    • Porter, S.C., North, A.K., Wedel, A.B., and Kustu, S. (1993). Oligomerization of NtrC at the glnA enhancer is required for transcriptional activation. Genes Dev. 7, 2258-2273.
    • (1993) Genes Dev. , vol.7 , pp. 2258-2273
    • Porter, S.C.1    North, A.K.2    Wedel, A.B.3    Kustu, S.4
  • 41
    • 0002830404 scopus 로고
    • Mechanism of transcriptional activation by NtrC (Nitrogen Regulatory Protein C): Requirement for oligomerization and phosphorylation
    • T. Silhavy and J. Hoch, eds. (Washington, D.C.: American Society of Microbiology)
    • Porter, S.C., North, A.K., and Kustu, S. (1995). Mechanism of transcriptional activation by NtrC (Nitrogen Regulatory Protein C): requirement for oligomerization and phosphorylation. In Two-Component Signal Transduction, T. Silhavy and J. Hoch, eds. (Washington, D.C.: American Society of Microbiology), pp. 147-158.
    • (1995) In Two-component Signal Transduction , pp. 147-158
    • Porter, S.C.1    North, A.K.2    Kustu, S.3
  • 42
    • 0022446209 scopus 로고
    • Transcription of glnA in E. Coli is stimulated by activator bound to sites far from the promoter
    • Reitzer, L., and Magasanik, B. (1986). Transcription of glnA in E. coli is stimulated by activator bound to sites far from the promoter. Cell 45, 785-792.
    • (1986) Cell , vol.45 , pp. 785-792
    • Reitzer, L.1    Magasanik, B.2
  • 44
    • 0024293495 scopus 로고
    • Identification of a novel lymphoid specific octamer binding protein (OTF-2B) by proteolytic clipping band-shift assay
    • Schreiber, E.P., Matthias, P., Muller, M.M., and Schaffner, W. (1988). Identification of a novel lymphoid specific octamer binding protein (OTF-2B) by proteolytic clipping band-shift assay. EMBO J. 7, 4221-4229.
    • (1988) EMBO J. , vol.7 , pp. 4221-4229
    • Schreiber, E.P.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 45
    • 0029670970 scopus 로고    scopus 로고
    • 54-dependent regulators: Derepression as a control mechanism
    • 54-dependent regulators: derepression as a control mechanism. Mol. Microbiol. 19, 409-416.
    • (1996) Mol. Microbiol. , vol.19 , pp. 409-416
    • Shingler, V.1
  • 46
    • 0028325759 scopus 로고
    • Sensing aromatic compounds by the DmpR transcriptional activator of phenol-catabolizing Pseudomonas sp. Strain CF600
    • Shingler, V., and Moore, T. (1994). Sensing aromatic compounds by the DmpR transcriptional activator of phenol-catabolizing Pseudomonas sp. strain CF600. J. Bacteriol. 176, 1555-1560.
    • (1994) J. Bacteriol. , vol.176 , pp. 1555-1560
    • Shingler, V.1    Moore, T.2
  • 47
    • 0029132191 scopus 로고
    • Direct regulation of the ATPase activity of the transcriptional activator DmpR by aromatic compounds
    • Shingler, V., and Pavel, H. (1995). Direct regulation of the ATPase activity of the transcriptional activator DmpR by aromatic compounds. Mol. Microbiol. 17, 505-513.
    • (1995) Mol. Microbiol. , vol.17 , pp. 505-513
    • Shingler, V.1    Pavel, H.2
  • 48
    • 0025035371 scopus 로고
    • DNA-looping and enhancer activity: Association between DNA-bound NtrC activator and RNA polymerase at the bacterial glnA promoter
    • Su, W., Porter, S.C., Kustu, S., and Echols, H. (1990). DNA-looping and enhancer activity: association between DNA-bound NtrC activator and RNA polymerase at the bacterial glnA promoter. Proc. Natl. Acad. Sci. USA 87, 5504-5508.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5504-5508
    • Su, W.1    Porter, S.C.2    Kustu, S.3    Echols, H.4
  • 49
    • 0025363427 scopus 로고
    • DNA binding-induced conformational change of the yeast transcriptional activator PRTF
    • Tan, S., and Richmond, T.J. (1990). DNA binding-induced conformational change of the yeast transcriptional activator PRTF. Cell 62, 367-377.
    • (1990) Cell , vol.62 , pp. 367-377
    • Tan, S.1    Richmond, T.J.2
  • 51
    • 0027128666 scopus 로고
    • The role of nucleoside triphosphate hydrolysis in transducing systems: P21 ras and muscle
    • Webb, M.R. (1992). The role of nucleoside triphosphate hydrolysis in transducing systems: p21 ras and muscle. Philos. Trans. R. Soc. Lond. Biol. 336, 19-24.
    • (1992) Philos. Trans. R. Soc. Lond. Biol. , vol.336 , pp. 19-24
    • Webb, M.R.1
  • 52
    • 0029166594 scopus 로고
    • The bacterial enhancer-binding protein NtrC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation
    • Wedel, A., and Kustu, S. (1995). The bacterial enhancer-binding protein NtrC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation. Genes Dev. 9, 2042-2052.
    • (1995) Genes Dev. , vol.9 , pp. 2042-2052
    • Wedel, A.1    Kustu, S.2
  • 53
    • 0026070143 scopus 로고
    • The phosphorylated form of the enhancer-binding protein NtrC has an ATPase activity that is essential for activation of transcription
    • Weiss, D., Batut, J., Klose, K., and Kustu, S. (1991). The phosphorylated form of the enhancer-binding protein NtrC has an ATPase activity that is essential for activation of transcription. Cell 67, 155-167.
    • (1991) Cell , vol.67 , pp. 155-167
    • Weiss, D.1    Batut, J.2    Klose, K.3    Kustu, S.4
  • 54
    • 0024403543 scopus 로고
    • The Q-linker: A class of interdomain sequences found in bacterial multidomain regulatory proteins
    • Wooton, J.C., and Drummond, M.H. (1989). The Q-linker: a class of interdomain sequences found in bacterial multidomain regulatory proteins. Protein Eng. 2, 535-543.
    • (1989) Protein Eng. , vol.2 , pp. 535-543
    • Wooton, J.C.1    Drummond, M.H.2
  • 55
    • 0028105752 scopus 로고
    • Identification of a putative alternate sigma factor and characterization of a multicomponent regulatory cascade controlling the expression of Pseudomonas syringae pv. Syringae Pss61 hrp and hrmA genes
    • Xiao,Y., Heu, S.,Yi, J., Lu, Y., and Hutcheson, S.W. (1994). Identification of a putative alternate sigma factor and characterization of a multicomponent regulatory cascade controlling the expression of Pseudomonas syringae pv. syringae Pss61 hrp and hrmA genes. J. Bacteriol. 176, 1025-1036
    • (1994) J. Bacteriol. , vol.176 , pp. 1025-1036
    • Heu, S.1    Yi, J.2    Lu, Y.3    Hutcheson, S.W.4


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