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Volumn 189, Issue 8, 2007, Pages 3017-3025

Ligand-controlled proteolysis of the Escherichia coli transcriptional regulator ZntR

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ARGININE; BACTERIAL DNA; ENDOPEPTIDASE LA; LIGAND; PROTEASE CLPXP; PROTEIN ZNTA; PROTEIN ZNTR; PROTEINASE; PROTEOME; REGULATOR PROTEIN; UNCLASSIFIED DRUG; ZINC;

EID: 34247844506     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01531-06     Document Type: Article
Times cited : (48)

References (47)
  • 1
    • 0038579426 scopus 로고    scopus 로고
    • Zn(II) metabolism in prokaryotes
    • Blencowe, D. K., and A. P. Morby. 2003. Zn(II) metabolism in prokaryotes. FEMS Microbiol. Rev. 27:291-311.
    • (2003) FEMS Microbiol. Rev , vol.27 , pp. 291-311
    • Blencowe, D.K.1    Morby, A.P.2
  • 3
    • 0033828371 scopus 로고    scopus 로고
    • Metal-ion tolerance in Escherichia coli: Analysis of transcriptional profiles by gene-array technology
    • Brocklehurst, K. R., and A. P. Morby. 2000. Metal-ion tolerance in Escherichia coli: analysis of transcriptional profiles by gene-array technology. Microbiology 146:2277-2282.
    • (2000) Microbiology , vol.146 , pp. 2277-2282
    • Brocklehurst, K.R.1    Morby, A.P.2
  • 7
    • 0442327287 scopus 로고    scopus 로고
    • Zinc resistance in bacteria
    • Choudhury, R., and S. Srivastava. 2001. Zinc resistance in bacteria. Curr. Sci. 81:768-775.
    • (2001) Curr. Sci , vol.81 , pp. 768-775
    • Choudhury, R.1    Srivastava, S.2
  • 9
    • 0026766977 scopus 로고
    • Zinc proteins: Enzymes, storage proteins, transcription factors, and replication proteins
    • Coleman, J. E. 1992. Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins. Annu. Rev. Biochem. 61:897-946.
    • (1992) Annu. Rev. Biochem , vol.61 , pp. 897-946
    • Coleman, J.E.1
  • 10
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 11
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn, J. M., S. B. Neher, Y. I. Kim, R. T. Sauer, and T. A. Baker. 2003. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 11:671-683.
    • (2003) Mol. Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 12
    • 14544304071 scopus 로고    scopus 로고
    • Regulated degradation of chromosome replication proteins DnaA and CtrA in Caulobacter crescentus
    • Gorbatyuk, B., and G. T. Marczynski. 2005. Regulated degradation of chromosome replication proteins DnaA and CtrA in Caulobacter crescentus. Mol. Microbiol. 55:1233-1245.
    • (2005) Mol. Microbiol , vol.55 , pp. 1233-1245
    • Gorbatyuk, B.1    Marczynski, G.T.2
  • 13
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacterial regulatory circuits
    • Gottesman, S. 2003. Proteolysis in bacterial regulatory circuits. Annu. Rev. Cell Dev. Biol. 19:565-587.
    • (2003) Annu. Rev. Cell Dev. Biol , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 14
    • 1642524483 scopus 로고    scopus 로고
    • Griffith, K. L., I. M. Shah, and R. E. Wolf, Jr. 2004. Proteolytic degradation of Escherichia coli transcription activators SoxS and MarA as the mechanism for reversing the induction of the superoxide (SoxRS) and multiple antibiotic resistance (Mar) regulons. Mol. Microbiol. 51:1801-1816.
    • Griffith, K. L., I. M. Shah, and R. E. Wolf, Jr. 2004. Proteolytic degradation of Escherichia coli transcription activators SoxS and MarA as the mechanism for reversing the induction of the superoxide (SoxRS) and multiple antibiotic resistance (Mar) regulons. Mol. Microbiol. 51:1801-1816.
  • 15
    • 7544239890 scopus 로고    scopus 로고
    • Fine-tuning of the Escherichia coli sigmaE envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA
    • Grigorova, I. L., R. Chaba, H. J. Zhong, B. M. Alba, V. Rhodius, C. Herman, and C. A. Gross. 2004. Fine-tuning of the Escherichia coli sigmaE envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA. Genes Dev. 18:2686-2697.
    • (2004) Genes Dev , vol.18 , pp. 2686-2697
    • Grigorova, I.L.1    Chaba, R.2    Zhong, H.J.3    Alba, B.M.4    Rhodius, V.5    Herman, C.6    Gross, C.A.7
  • 16
    • 0035696323 scopus 로고    scopus 로고
    • Bacterial zinc transporters and regulators
    • Hantke, K. 2001. Bacterial zinc transporters and regulators. Biometals 14:239-249.
    • (2001) Biometals , vol.14 , pp. 239-249
    • Hantke, K.1
  • 17
    • 0141789762 scopus 로고    scopus 로고
    • Proteolysis in prokaryotes: Protein quality control and regulatory principles
    • Hengge, R., and B. Bukau. 2003. Proteolysis in prokaryotes: protein quality control and regulatory principles. Mol. Microbiol. 49:1451-1462.
    • (2003) Mol. Microbiol , vol.49 , pp. 1451-1462
    • Hengge, R.1    Bukau, B.2
  • 18
    • 32244435782 scopus 로고    scopus 로고
    • Two peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAP
    • Hoskins, J. R., and S. Wickner. 2006. Two peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAP. Proc. Natl. Acad. Sci. USA 103:909-914.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 909-914
    • Hoskins, J.R.1    Wickner, S.2
  • 19
    • 0022051541 scopus 로고
    • The use of 4-(2-pyridylazo)-resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
    • Hunt, J. B., S. H. Neece, and A. Ginsburg. 1985. The use of 4-(2-pyridylazo)-resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase. Anal. Biochem. 146:150-157.
    • (1985) Anal. Biochem , vol.146 , pp. 150-157
    • Hunt, J.B.1    Neece, S.H.2    Ginsburg, A.3
  • 20
    • 0035448390 scopus 로고    scopus 로고
    • Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine
    • Ishii, Y., and F. Amano. 2001. Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine. Biochem. J. 358:473-480.
    • (2001) Biochem. J , vol.358 , pp. 473-480
    • Ishii, Y.1    Amano, F.2
  • 21
    • 0038690474 scopus 로고    scopus 로고
    • Regulation by proteolysis in bacterial cells
    • Jenal, U., and R. Hengge-Aronis. 2003. Regulation by proteolysis in bacterial cells. Curr. Opin. Microbiol. 6:163-172.
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 163-172
    • Jenal, U.1    Hengge-Aronis, R.2
  • 22
    • 26244460528 scopus 로고    scopus 로고
    • Engulfment-regulated proteolysis of SpoIIQ: Evidence that dual checkpoints control sigma activity
    • Jiang, X., A. Rubio, S. Chiba, and K. Pogliano. 2005. Engulfment-regulated proteolysis of SpoIIQ: evidence that dual checkpoints control sigma activity. Mol. Microbiol. 58:102-115.
    • (2005) Mol. Microbiol , vol.58 , pp. 102-115
    • Jiang, X.1    Rubio, A.2    Chiba, S.3    Pogliano, K.4
  • 23
    • 0036434580 scopus 로고    scopus 로고
    • The functional analysis of directed amino-acid alterations in ZntR from Escherichia coli
    • Khan, S., K. R. Brocklehurst, G. W. Jones, and A. P. Morby. 2002. The functional analysis of directed amino-acid alterations in ZntR from Escherichia coli. Biochem. Biophys. Res. Commun. 299:438-445.
    • (2002) Biochem. Biophys. Res. Commun , vol.299 , pp. 438-445
    • Khan, S.1    Brocklehurst, K.R.2    Jones, G.W.3    Morby, A.P.4
  • 24
    • 0033638255 scopus 로고    scopus 로고
    • Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
    • Kim, Y. I., R. E. Burton, B. M. Burton, R. T. Sauer, and T. A. Baker. 2000. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol. Cell 5:639-648.
    • (2000) Mol. Cell , vol.5 , pp. 639-648
    • Kim, Y.I.1    Burton, R.E.2    Burton, B.M.3    Sauer, R.T.4    Baker, T.A.5
  • 25
    • 0035930564 scopus 로고    scopus 로고
    • Copper-induced proteolysis of the CopZ copper chaperone of Enterococcus hirae
    • Lu, Z. H., and M. Solioz. 2001. Copper-induced proteolysis of the CopZ copper chaperone of Enterococcus hirae. J. Biol. Chem. 276:47822-47827.
    • (2001) J. Biol. Chem , vol.276 , pp. 47822-47827
    • Lu, Z.H.1    Solioz, M.2
  • 26
    • 27644589698 scopus 로고    scopus 로고
    • ClpXP-dependent proteolysis of FNR upon loss of its O2-sensing [4Fe-4S] cluster
    • Mettert, E. L., and P. J. Kiley. 2005. ClpXP-dependent proteolysis of FNR upon loss of its O2-sensing [4Fe-4S] cluster. J. Mol. Biol. 354:220-232.
    • (2005) J. Mol. Biol , vol.354 , pp. 220-232
    • Mettert, E.L.1    Kiley, P.J.2
  • 28
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera, O. D., C. M. Kay, and R. S. Hodges. 1994. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3:1984-1991.
    • (1994) Protein Sci , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 29
    • 33646021005 scopus 로고    scopus 로고
    • Proteomic profiling of ClpXP substrates after DNA damage reveals extensive instability within SOS regulon
    • Neher, S. B., J. Villen, E. C. Oakes, C. E. Bakalarski, R. T. Sauer, S. P. Gygi, and T. A. Baker. 2006. Proteomic profiling of ClpXP substrates after DNA damage reveals extensive instability within SOS regulon. Mol. Cell 22:193-204.
    • (2006) Mol. Cell , vol.22 , pp. 193-204
    • Neher, S.B.1    Villen, J.2    Oakes, E.C.3    Bakalarski, C.E.4    Sauer, R.T.5    Gygi, S.P.6    Baker, T.A.7
  • 30
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten, C. E., and T. V. O'Halloran. 2001. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292:2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 31
    • 0033621407 scopus 로고    scopus 로고
    • DNA distortion mechanism for transcriptional activation by ZntR, a Zn(II)-responsive MerR homologue in Escherichia coli
    • Outten, C. E., F. W. Outten, and T. V. O'Halloran. 1999. DNA distortion mechanism for transcriptional activation by ZntR, a Zn(II)-responsive MerR homologue in Escherichia coli. J. Biol. Chem. 274:37517- 37524.
    • (1999) J. Biol. Chem , vol.274 , pp. 37517-37524
    • Outten, C.E.1    Outten, F.W.2    O'Halloran, T.V.3
  • 32
    • 0027500239 scopus 로고
    • Construction and characterization of a mercury-independent MerR activator (MerRAC): Transcriptional activation in the absence of Hg(II) is accompanied by DNA distortion
    • Parkhill, J., A. Z. Ansari, J. G. Wright, N. L. Brown, and T. V. O'Halloran. 1993. Construction and characterization of a mercury-independent MerR activator (MerRAC): transcriptional activation in the absence of Hg(II) is accompanied by DNA distortion. EMBO J. 12:413-421.
    • (1993) EMBO J , vol.12 , pp. 413-421
    • Parkhill, J.1    Ansari, A.Z.2    Wright, J.G.3    Brown, N.L.4    O'Halloran, T.V.5
  • 33
    • 0034637471 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli
    • Patzer, S. I., and K. Hantke. 2000. The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli. J. Biol. Chem. 275:24321-24332.
    • (2000) J. Biol. Chem , vol.275 , pp. 24321-24332
    • Patzer, S.I.1    Hantke, K.2
  • 34
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • Patzer, S. I., and K. Hantke. 1998. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol. 28:1199-1210.
    • (1998) Mol. Microbiol , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 35
    • 0028604471 scopus 로고    scopus 로고
    • Powell, B. S., M. P. Rivas, D. L. Court, Y. Nakamura, and C. L. Turnbough, Jr. 1994. Rapid confirmation of single copy lambda prophage integration by PCR. Nucleic Acids Res. 22:5765-5766.
    • Powell, B. S., M. P. Rivas, D. L. Court, Y. Nakamura, and C. L. Turnbough, Jr. 1994. Rapid confirmation of single copy lambda prophage integration by PCR. Nucleic Acids Res. 22:5765-5766.
  • 36
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • Prakash, S., L. Tian, K. S. Ratliff, R. E. Lehotzky, and A. Matouschek. 2004. An unstructured initiation site is required for efficient proteasome-mediated degradation. Nat. Struct. Mol. Biol. 11:830-837.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 37
    • 0031475157 scopus 로고    scopus 로고
    • The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase
    • Rensing, C., B. Mitra, and B. P. Rosen. 1997. The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. Proc. Natl. Acad. Sci. USA 94:14326-14331.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14326-14331
    • Rensing, C.1    Mitra, B.2    Rosen, B.P.3
  • 40
    • 33644839119 scopus 로고    scopus 로고
    • Shah, I. M., and R. E. Wolf, Jr. 2006. Inhibition of Lon-dependent degradation of the Escherichia coli transcription activator SoxS by interaction with 'soxbox' DNA or RNA polymerase. Mol. Microbiol. 60:199-208.
    • Shah, I. M., and R. E. Wolf, Jr. 2006. Inhibition of Lon-dependent degradation of the Escherichia coli transcription activator SoxS by interaction with 'soxbox' DNA or RNA polymerase. Mol. Microbiol. 60:199-208.
  • 41
    • 33644935094 scopus 로고    scopus 로고
    • Shah, I. M., and R. E. Wolf, Jr. 2006. Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-terminal 21 amino acid residues. J. Mol. Biol. 357:718-731.
    • Shah, I. M., and R. E. Wolf, Jr. 2006. Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-terminal 21 amino acid residues. J. Mol. Biol. 357:718-731.
  • 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
    • 0032538886 scopus 로고    scopus 로고
    • Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor
    • Turgay, K., J. Hahn, J. Burghoorn, and D. Dubnau. 1998. Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor. EMBO J. 17:6730-6738.
    • (1998) EMBO J , vol.17 , pp. 6730-6738
    • Turgay, K.1    Hahn, J.2    Burghoorn, J.3    Dubnau, D.4
  • 45
    • 0028985721 scopus 로고
    • Protection of coliphage lambda O initiator protein from proteolysis in the assembly of the replication complex in vivo
    • Wegrzyn, A., G. Wegrzyn, and K. Taylor. 1995. Protection of coliphage lambda O initiator protein from proteolysis in the assembly of the replication complex in vivo. Virology 207:179-184.
    • (1995) Virology , vol.207 , pp. 179-184
    • Wegrzyn, A.1    Wegrzyn, G.2    Taylor, K.3
  • 46
    • 24944583149 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external zinc
    • Yamamoto, K., and A. Ishihama. 2005. Transcriptional response of Escherichia coli to external zinc. J. Bacteriol. 187:6333-6340.
    • (2005) J. Bacteriol , vol.187 , pp. 6333-6340
    • Yamamoto, K.1    Ishihama, A.2
  • 47
    • 0031893254 scopus 로고    scopus 로고
    • Copper differentially regulates the activity and degradation of yeast Mac1 transcription factor
    • Zhu, Z., S. Labbe, M. M. Pena, and D. J. Thiele. 1998. Copper differentially regulates the activity and degradation of yeast Mac1 transcription factor. J. Biol. Chem. 273:1277-1280.
    • (1998) J. Biol. Chem , vol.273 , pp. 1277-1280
    • Zhu, Z.1    Labbe, S.2    Pena, M.M.3    Thiele, D.J.4


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