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Volumn 182, Issue 2, 2000, Pages 311-319

The PspA protein of Escherichia coli is a negative regulator of σ54- dependent transcription

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; BINDING PROTEIN; PROTEIN PSPA; RNA POLYMERASE; SIGMA FACTOR; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0033986477     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.2.311-319.2000     Document Type: Article
Times cited : (80)

References (48)
  • 1
    • 0027261284 scopus 로고
    • Structure, function and application of the coiled-coil protein folding motif
    • Adamson, J. G., N. E. Zhou, and R. S. Hodges. 1993. Structure, function and application of the coiled-coil protein folding motif. Curr. Opin. Biotechnol. 4:428-437.
    • (1993) Curr. Opin. Biotechnol. , vol.4 , pp. 428-437
    • Adamson, J.G.1    Zhou, N.E.2    Hodges, R.S.3
  • 2
    • 0028264349 scopus 로고
    • Purification and in vitro activities of the native nitrogen fixation control proteins NifA and NifL
    • Austin, S., M. Buck, W. Cannon, T. Eydmann, and R. Dixon. 1994. Purification and in vitro activities of the native nitrogen fixation control proteins NifA and NifL. J. Bacteriol. 176:3460-3465.
    • (1994) J. Bacteriol. , vol.176 , pp. 3460-3465
    • Austin, S.1    Buck, M.2    Cannon, W.3    Eydmann, T.4    Dixon, R.5
  • 3
    • 0026519885 scopus 로고
    • Mutations of the phage lambda nutL region that prevent the action of Nun, a site-specific transcription termination factor
    • Baron, J., and R. A. Weisberg. 1992. Mutations of the phage lambda nutL region that prevent the action of Nun, a site-specific transcription termination factor. J. Bacteriol. 174:1983-1989.
    • (1992) J. Bacteriol. , vol.174 , pp. 1983-1989
    • Baron, J.1    Weisberg, R.A.2
  • 4
    • 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., F. Narberhaus, and S. Kustu. 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
  • 5
    • 0019308328 scopus 로고
    • Positive selection for loss of tetracycline resistance
    • Bochner, B. R., H. C. Huang, G. L. Schieven, and B. N. Ames. 1980. Positive selection for loss of tetracycline resistance. J. Bacteriol. 143:925-933.
    • (1980) J. Bacteriol. , vol.143 , pp. 925-933
    • Bochner, B.R.1    Huang, H.C.2    Schieven, G.L.3    Ames, B.N.4
  • 7
    • 0025830893 scopus 로고
    • Characterization and sequence of the Escherichia coli stress-induced psp operon
    • Brissette, J. L., L. Weiner, T. L. Ripmaster, and P. Model. 1991. Characterization and sequence of the Escherichia coli stress-induced psp operon. J. Mol. Biol. 220:35-48.
    • (1991) J. Mol. Biol. , vol.220 , pp. 35-48
    • Brissette, J.L.1    Weiner, L.2    Ripmaster, T.L.3    Model, P.4
  • 8
    • 0029070395 scopus 로고
    • The role of anti-sigma factors in gene regulation
    • Brown, K. L., and K. T. Hughes. 1995. The role of anti-sigma factors in gene regulation. Mol. Microbiol. 16:397-404.
    • (1995) Mol. Microbiol. , vol.16 , pp. 397-404
    • Brown, K.L.1    Hughes, K.T.2
  • 9
    • 0018959055 scopus 로고
    • In vitro gene fusions that join an enzymatically active beta-galactosidase segment to amino-terminal fragments of exogenous proteins: Escherichia coli plasmid vectors for the detection and cloning of translational initiation signals
    • Casadaban, M. J., J. Chou, and S. N. Cohen. 1980. In vitro gene fusions that join an enzymatically active beta-galactosidase segment to amino-terminal fragments of exogenous proteins: Escherichia coli plasmid vectors for the detection and cloning of translational initiation signals. J. Bacteriol. 143:971-980.
    • (1980) J. Bacteriol. , vol.143 , pp. 971-980
    • Casadaban, M.J.1    Chou, J.2    Cohen, S.N.3
  • 10
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P. Y., and G. D. Fasman. 1974. Prediction of protein conformation. Biochemistry 13:222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 11
    • 0025971243 scopus 로고
    • Role of integration host factor in the regulation of the glnHp2 promoter of Escherichia coli
    • Claverie-Martin, F., and B. Magasanik. 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
  • 12
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: The dense alignment surface method
    • Cserzo, M., E. Wallin, I. Simon, G. von Heijne, and A. Elofsson. 1997. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng. 10:673-676.
    • (1997) Protein Eng. , vol.10 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 13
    • 0030775809 scopus 로고    scopus 로고
    • Role of upstream activation sequences and integration host factor in transcriptional activation by the constitutively active prokaryotic enhancer-binding protein PspF
    • Dworkin, J., G. Jovanovic, and P. Model. 1997. Role of upstream activation sequences and integration host factor in transcriptional activation by the constitutively active prokaryotic enhancer-binding protein PspF. J. Mol. Biol. 273:377-388.
    • (1997) J. Mol. Biol. , vol.273 , pp. 377-388
    • Dworkin, J.1    Jovanovic, G.2    Model, P.3
  • 14
    • 0029591598 scopus 로고
    • Repression of the Klebsiella aerogenes nac promoter
    • Feng, J., T. J. Goss, R. A. Bender, and A. J. Ninfa. 1995. Repression of the Klebsiella aerogenes nac promoter. J. Bacteriol. 177:5535-5538.
    • (1995) J. Bacteriol. , vol.177 , pp. 5535-5538
    • Feng, J.1    Goss, T.J.2    Bender, R.A.3    Ninfa, A.J.4
  • 15
    • 0029063837 scopus 로고
    • Activation of the transcriptional regulator XyIR of Pseudomonas putida by release of repression between functional domains
    • Fernandez, S., V. de Lorenzo, and J. Perez-Martin. 1995. Activation of the transcriptional regulator XyIR of Pseudomonas putida by release of repression between functional domains. Mol. Microbiol. 16:205-213.
    • (1995) Mol. Microbiol. , vol.16 , pp. 205-213
    • Fernandez, S.1    De Lorenzo, V.2    Perez-Martin, J.3
  • 16
    • 0029744180 scopus 로고    scopus 로고
    • Cold shock stress-induced proteins in Bacillus subtilis
    • Graumann, P., K. Schroder, R. Schmid, and M. A. Marahiel. 1996. Cold shock stress-induced proteins in Bacillus subtilis. J. Bacteriol. 178:4611-4619.
    • (1996) J. Bacteriol. , vol.178 , pp. 4611-4619
    • Graumann, P.1    Schroder, K.2    Schmid, R.3    Marahiel, M.A.4
  • 17
    • 0001645845 scopus 로고
    • Role of metal ions in negative regulation of nitrogen fixation by the nifL product from Klebsiella pneumoniae
    • Henderson, N., S. A. Austin, and R. A. Dixon. 1989. Role of metal ions in negative regulation of nitrogen fixation by the nifL product from Klebsiella pneumoniae. Mol. Gen. Genet. 216:484-491.
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 484-491
    • Henderson, N.1    Austin, S.A.2    Dixon, R.A.3
  • 18
    • 0025598302 scopus 로고
    • Sequence requirements for coiled-coils: Analysis with lambda repressor-GCN4 leucine zipper fusions
    • Hu, J. C., E. K. O'Shea, P. S. Kim, and R. T. Sauer. 1990. Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions. Science 250:1400-1403.
    • (1990) Science , vol.250 , pp. 1400-1403
    • Hu, J.C.1    O'Shea, E.K.2    Kim, P.S.3    Sauer, R.T.4
  • 19
    • 0030855599 scopus 로고    scopus 로고
    • Autogenous control of PspF, the constitutively active enhancer-binding protein of Escherichia coli
    • Jovanovic, G., J. Dworkin, and P. Model. 1997. Autogenous control of PspF, the constitutively active enhancer-binding protein of Escherichia coli. J. Bacteriol. 179:5232-5237.
    • (1997) J. Bacteriol. , vol.179 , pp. 5232-5237
    • Jovanovic, G.1    Dworkin, J.2    Model, P.3
  • 20
    • 0030881602 scopus 로고    scopus 로고
    • PspF and IHF bind cooperatively in the psp promoter-regulatory region of Escherichia coli
    • Jovanovic, G., and P. Model. 1997. PspF and IHF bind cooperatively in the psp promoter-regulatory region of Escherichia coli. Mol. Microbiol. 25:473-481.
    • (1997) Mol. Microbiol. , vol.25 , pp. 473-481
    • Jovanovic, G.1    Model, P.2
  • 21
    • 0033555834 scopus 로고    scopus 로고
    • 54 transcription activator, PspF, and its DNA-binding mutant, PspFΔHTH
    • 54 transcription activator, PspF, and its DNA-binding mutant, PspFΔHTH. J. Mol. Biol. 285:469-483.
    • (1999) J. Mol. Biol. , vol.285 , pp. 469-483
    • Jovanovic, G.1    Rakonjac, J.2    Model, P.3
  • 22
    • 0029874910 scopus 로고    scopus 로고
    • Identification, nucleotide sequence, and characterization of PspF, the transcriptional activator of the Escherichia coli stress-induced psp operon
    • Jovanovic, G., L. Weiner, and P. Model. 1996. Identification, nucleotide sequence, and characterization of PspF, the transcriptional activator of the Escherichia coli stress-induced psp operon. J. Bacteriol. 178:1936-1945.
    • (1996) J. Bacteriol. , vol.178 , pp. 1936-1945
    • Jovanovic, G.1    Weiner, L.2    Model, P.3
  • 23
    • 0029655167 scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome (supplement)
    • Kaneko, T., A. Tanaka, S. Sato, H. Kotani, T. Sazuka, N. Miyajima, M. Sugiura, and S. Tabata. 1995. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome (supplement). DNA Res. 2:191-198.
    • (1995) DNA Res. , vol.2 , pp. 191-198
    • Kaneko, T.1    Tanaka, A.2    Sato, S.3    Kotani, H.4    Sazuka, T.5    Miyajima, N.6    Sugiura, M.7    Tabata, S.8
  • 24
    • 0030028862 scopus 로고    scopus 로고
    • Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions
    • Kleerebezem, M., W. Crielaard, and J. Tommassen. 1996. Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions. EMBO J. 15:162-171.
    • (1996) EMBO J. , vol.15 , pp. 162-171
    • Kleerebezem, M.1    Crielaard, W.2    Tommassen, J.3
  • 25
    • 0027522364 scopus 로고
    • Expression of the pspA gene stimulates efficient protein export in Escherichia coli
    • Kleerebezem, M., and J. Tommassen. 1993. Expression of the pspA gene stimulates efficient protein export in Escherichia coli. Mol. Microbiol. 7:947-956.
    • (1993) Mol. Microbiol. , vol.7 , pp. 947-956
    • Kleerebezem, M.1    Tommassen, J.2
  • 26
    • 0343457347 scopus 로고
    • Ph.D. thesis, Cambridge University, Cambridge, United Kingdom
    • Knight, A. E. 1994. Ph.D. thesis, Cambridge University, Cambridge, United Kingdom.
    • (1994)
    • Knight, A.E.1
  • 28
    • 0025938894 scopus 로고
    • Prokaryotic transcriptional enhancers and enhancer-binding proteins
    • Kustu, S., A. K. North, and D. S. Weiss. 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.S.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0027497044 scopus 로고
    • In vitro activity of NifL, a signal transduction protein for biological nitrogen fixation
    • Lee, H. S., F. Narberhaus, and S. Kustu. 1993. In vitro activity of NifL, a signal transduction protein for biological nitrogen fixation. J. Bacteriol. 175: 7683-7688.
    • (1993) J. Bacteriol. , vol.175 , pp. 7683-7688
    • Lee, H.S.1    Narberhaus, F.2    Kustu, S.3
  • 31
    • 0028839628 scopus 로고
    • Protein crosslinking studies suggest that Rhizobium meliloti C4-dicarboxylic acid transport protein D, a sigma 54-dependent transcriptional activator, interacts with sigma 54 and the beta subunit of RNA polymerase
    • Lee, J. H., and T. R. Hoover. 1995. Protein crosslinking studies suggest that Rhizobium meliloti C4-dicarboxylic acid transport protein D, a sigma 54-dependent transcriptional activator, interacts with sigma 54 and the beta subunit of RNA polymerase. Proc. Natl. Acad. Sci. USA 92:9702-9706.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9702-9706
    • Lee, J.H.1    Hoover, T.R.2
  • 32
    • 0026680833 scopus 로고
    • Dissection of IncP conjugative plasmid transfer: Definition of the transfer region Tra2 by mobilization of the Tra1 region in trans
    • Lessl, M., D. Balzer, R. Lurz, V. L. Waters, D. G. Guiney, and E. Lanka. 1992. Dissection of IncP conjugative plasmid transfer: definition of the transfer region Tra2 by mobilization of the Tra1 region in trans. J. Bacteriol. 174:2493-2500.
    • (1992) J. Bacteriol. , vol.174 , pp. 2493-2500
    • Lessl, M.1    Balzer, D.2    Lurz, R.3    Waters, V.L.4    Guiney, D.G.5    Lanka, E.6
  • 33
    • 0028467779 scopus 로고
    • Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes
    • Li, H. M., Y. Kaneko, and K. Keegstra. 1994. Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes. Plant Mol. Biol. 25:619-632.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 619-632
    • Li, H.M.1    Kaneko, Y.2    Keegstra, K.3
  • 34
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 36
    • 0024240949 scopus 로고
    • The DNA-binding domain of the transcriptional activator protein NifA resides in its carboxy terminus, recognises the upstream activator sequences of nif promoters and can be separated from the positive control function of NifA
    • Morett, E., W. Cannon, and M. Buck. 1988. The DNA-binding domain of the transcriptional activator protein NifA resides in its carboxy terminus, recognises the upstream activator sequences of nif promoters and can be separated from the positive control function of NifA. Nucleic Acids Res. 16: 11469-11488.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 11469-11488
    • Morett, E.1    Cannon, W.2    Buck, M.3
  • 37
    • 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 B. Magasanik. 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
  • 38
    • 0030602821 scopus 로고    scopus 로고
    • ATP binding to the sigma 54-dependent activator XyIR triggers a protein multimerization cycle catalyzed by UAS DNA
    • Perez-Martin, J., and V. de Lorenzo. 1996. ATP binding to the sigma 54-dependent activator XyIR triggers a protein multimerization cycle catalyzed by UAS DNA. Cell 86:331-339.
    • (1996) Cell , vol.86 , pp. 331-339
    • Perez-Martin, J.1    De Lorenzo, V.2
  • 39
    • 0026910385 scopus 로고
    • Immobilized metal ion affinity chromatography
    • Porath, J. 1992. Immobilized metal ion affinity chromatography. Protein Expr. Purif. 3:263-281.
    • (1992) Protein Expr. Purif. , vol.3 , pp. 263-281
    • Porath, J.1
  • 40
    • 0027359777 scopus 로고
    • Oligomerization of NTRC at the glnA enhancer is required for transcriptional activation
    • Porter, S. C., A. K. North, A. B. Wedel, and S. Kustu. 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
  • 43
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R. W., F. Houman, and N. Kleckner. 1987. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53:85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 44
    • 0026091833 scopus 로고
    • Stress-induced expression of the Escherichia coli phage shock protein operon is dependent on sigma 54 and modulated by positive and negative feedback mechanisms
    • Weiner, L., J. L. Brissette, and P. Model. 1991. Stress-induced expression of the Escherichia coli phage shock protein operon is dependent on sigma 54 and modulated by positive and negative feedback mechanisms. Genes Dev. 5:1912-1923.
    • (1991) Genes Dev. , vol.5 , pp. 1912-1923
    • Weiner, L.1    Brissette, J.L.2    Model, P.3
  • 45
    • 0028293317 scopus 로고
    • Role of an Escherichia coli stress-response operon in stationary-phase survival
    • Weiner, L., and P. Model. 1994. Role of an Escherichia coli stress-response operon in stationary-phase survival. Proc. Natl. Acad. Sci. USA 91:2191-2195.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2191-2195
    • Weiner, L.1    Model, P.2
  • 46
    • 0021992336 scopus 로고
    • Site-directed insertion and deletion mutagenesis with cloned fragments in Escherichia coli
    • Winans, S. C., S. J. Elledge, J. H. Krueger, and G. C. Walker. 1985. Site-directed insertion and deletion mutagenesis with cloned fragments in Escherichia coli. J. Bacteriol. 161:1219-1221.
    • (1985) J. Bacteriol. , vol.161 , pp. 1219-1221
    • Winans, S.C.1    Elledge, S.J.2    Krueger, J.H.3    Walker, G.C.4
  • 47
    • 0030894489 scopus 로고    scopus 로고
    • Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein
    • Wyman, C., I. Rombel, A. K. North, C. Bustamante, and S. Kustu. 1997. Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein. Science 275:1658-1661.
    • (1997) Science , vol.275 , pp. 1658-1661
    • Wyman, C.1    Rombel, I.2    North, A.K.3    Bustamante, C.4    Kustu, S.5
  • 48
    • 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., S. Heu, J. Yi, Y. Lu, and S. W. Hutcheson. 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
    • Xiao, Y.1    Heu, S.2    Yi, J.3    Lu, Y.4    Hutcheson, S.W.5


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