메뉴 건너뛰기




Volumn 52, Issue 2, 2004, Pages 427-435

Dispensable PDZ domain of Escherichia coli YaeL essential protease

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CELL VIABILITY; CONTROLLED STUDY; CYTOPLASM; ENZYME DEGRADATION; ESCHERICHIA COLI; GENE DELETION; GENE MUTATION; MEMBRANE TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION;

EID: 1942468856     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.03985.x     Document Type: Article
Times cited : (36)

References (32)
  • 1
    • 0033568606 scopus 로고    scopus 로고
    • The Escherichia coli sigma (E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor
    • Ades, S.E., Connolly, L.E., Alba, B.M., and Gross, C.A. (1999) The Escherichia coli sigma (E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor. Genes Dev 13: 2449-2461.
    • (1999) Genes Dev , vol.13 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 2
    • 0034933064 scopus 로고    scopus 로고
    • DegS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity
    • Alba, B.M., Zhong, H.J., Pelayo, J.C., and Gross, C.A. (2001) degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity. Mol Microbiol 40: 1323-1333.
    • (2001) Mol Microbiol , vol.40 , pp. 1323-1333
    • Alba, B.M.1    Zhong, H.J.2    Pelayo, J.C.3    Gross, C.A.4
  • 3
    • 0037102509 scopus 로고    scopus 로고
    • DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma (E)-dependent extracytoplasmic stress response
    • Alba, B.M., Leeds, J.A., Onufryk, C., Lu, C.Z., and Gross, C.A. (2002) DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma (E)-dependent extracytoplasmic stress response. Genes Dev 16: 2156-2168.
    • (2002) Genes Dev , vol.16 , pp. 2156-2168
    • Alba, B.M.1    Leeds, J.A.2    Onufryk, C.3    Lu, C.Z.4    Gross, C.A.5
  • 5
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown, M.S.YeJ., Rawson, R.B., and Goldstein, J.L. (2000) Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100: 391-398.
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.Y.1    Rawson, R.B.2    Goldstein, J.L.3
  • 6
    • 0036364355 scopus 로고    scopus 로고
    • Competition between SsrA tagging and translational termination at weak stop codons in Escherichia coli
    • Collier, J., Binet, E., and Bouloc, P. (2002) Competition between SsrA tagging and translational termination at weak stop codons in Escherichia coli. Mol Microbiol 45: 745-754.
    • (2002) Mol Microbiol , vol.45 , pp. 745-754
    • Collier, J.1    Binet, E.2    Bouloc, P.3
  • 7
    • 0035503217 scopus 로고    scopus 로고
    • EcfE, a new essential inner membrane protease: Its role in the regulation of heat shock response in Escherichia coli
    • Dartigalongue, C., Loferer, H., and Raina, S. (2001a) EcfE, a new essential inner membrane protease: its role in the regulation of heat shock response in Escherichia coli. EMBO J 20: 5908-5918.
    • (2001) EMBO J , vol.20 , pp. 5908-5918
    • Dartigalongue, C.1    Loferer, H.2    Raina, S.3
  • 8
    • 0035877593 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli sigma e regulon
    • Dartigalongue, C., Missiakas, D., and Raina, S. (2001b) Characterization of the Escherichia coli sigma E regulon. J Biol Chem 276: 20866-20875.
    • (2001) J Biol Chem , vol.276 , pp. 20866-20875
    • Dartigalongue, C.1    Missiakas, D.2    Raina, S.3
  • 9
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (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
  • 10
    • 0030611303 scopus 로고    scopus 로고
    • The sigmaE-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigmaE
    • De Las Penas, A., Connolly, L., and Gross, C.A. (1997) The sigmaE-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigmaE. Mol Microbiol 24: 373-385.
    • (1997) Mol Microbiol , vol.24 , pp. 373-385
    • De Las Penas, A.1    Connolly, L.2    Gross, C.A.3
  • 11
    • 0026769761 scopus 로고
    • New cloning vectors for integration in the lambda attachment site attB of the Escherichia coli chromosome
    • Diederich, L., Rasmussen, L.J., and Messer, W. (1992) New cloning vectors for integration in the lambda attachment site attB of the Escherichia coli chromosome. Plasmid 28: 14-24.
    • (1992) Plasmid , vol.28 , pp. 14-24
    • Diederich, L.1    Rasmussen, L.J.2    Messer, W.3
  • 12
    • 0035975859 scopus 로고    scopus 로고
    • The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins
    • Einhauer, A., and Jungbauer, A. (2001) The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins. J Biochem Biophys Meth 49: 455-465.
    • (2001) J Biochem Biophys Meth , vol.49 , pp. 455-465
    • Einhauer, A.1    Jungbauer, A.2
  • 13
    • 0036786221 scopus 로고    scopus 로고
    • Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: The Papa pilin
    • Jones, C.H., Dexter, P., Evans, A.K., Liu, C., Hultgren, S.J., and Hruby, D.E. (2002) Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin. J Bacteriol 184: 5762-5771.
    • (2002) J Bacteriol , vol.184 , pp. 5762-5771
    • Jones, C.H.1    Dexter, P.2    Evans, A.K.3    Liu, C.4    Hultgren, S.J.5    Hruby, D.E.6
  • 14
    • 0035960904 scopus 로고    scopus 로고
    • Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli
    • Kanehara, K., Akiyama, Y., and Ito, K. (2001) Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli. Gene 281: 71-79.
    • (2001) Gene , vol.281 , pp. 71-79
    • Kanehara, K.1    Akiyama, Y.2    Ito, K.3
  • 15
    • 0037102458 scopus 로고    scopus 로고
    • YaeL (EcfE) activates the sigma (E) pathway of stress response through a site-2 cleavage of anti-sigma (E), RseA
    • Kanehara, K., Ito, K., and Akiyama, Y. (2002) YaeL (EcfE) activates the sigma (E) pathway of stress response through a site-2 cleavage of anti-sigma (E), RseA. Genes Dev 16: 2147-2155.
    • (2002) Genes Dev , vol.16 , pp. 2147-2155
    • Kanehara, K.1    Ito, K.2    Akiyama, Y.3
  • 16
    • 0032965585 scopus 로고    scopus 로고
    • A novel clan of zinc metallopeptidases with possible intramembrane cleavage properties
    • Lewis, A.P., and Thomas, P.J. (1999) A novel clan of zinc metallopeptidases with possible intramembrane cleavage properties. Protein Sci 8: 439-442.
    • (1999) Protein Sci , vol.8 , pp. 439-442
    • Lewis, A.P.1    Thomas, P.J.2
  • 17
    • 0030796260 scopus 로고    scopus 로고
    • Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: Application to open reading frame characterization
    • Link, A.J., Phillips, D., and Church, G.M. (1997) Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization. J Bacteriol 179: 6228-6237.
    • (1997) J Bacteriol , vol.179 , pp. 6228-6237
    • Link, A.J.1    Phillips, D.2    Church, G.M.3
  • 18
    • 0030861452 scopus 로고    scopus 로고
    • Independent and tight regulation of transcriptional units in Escherichia coli via the LacR/O, the TetR/O and AraC/I1-I2 regulatory elements
    • Lutz, R., and Bujard, H. (1997) Independent and tight regulation of transcriptional units in Escherichia coli via the LacR/O, the TetR/O and AraC/I1-I2 regulatory elements. Nucleic Acids Res 25: 1203-1210.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1203-1210
    • Lutz, R.1    Bujard, H.2
  • 19
    • 0027787823 scopus 로고
    • The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins
    • Issn: 0890-9369.
    • Mecsas, J., Rouviere, P.E., Erickson, J.W., Donohue, T.J., and Gross, C.A. (1993) The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins. Genes Dev 7: 2618-2628 Issn: 0890-9369.
    • (1993) Genes Dev , vol.7 , pp. 2618-2628
    • Mecsas, J.1    Rouviere, P.E.2    Erickson, J.W.3    Donohue, T.J.4    Gross, C.A.5
  • 21
    • 0030907038 scopus 로고    scopus 로고
    • Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins
    • Missiakas, D., Mayer, M.P., Lemaire, M., Georgopoulos, C., and Raina, S. (1997) Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol Microbiol 24: 355-371.
    • (1997) Mol Microbiol , vol.24 , pp. 355-371
    • Missiakas, D.1    Mayer, M.P.2    Lemaire, M.3    Georgopoulos, C.4    Raina, S.5
  • 22
    • 0031745718 scopus 로고    scopus 로고
    • The extracytoplasmic function sigma factors: Role and regulation
    • Missiakas, D., and Raina, S. (1998) The extracytoplasmic function sigma factors: role and regulation. Mol Microbiol 28: 1059-1066.
    • (1998) Mol Microbiol , vol.28 , pp. 1059-1066
    • Missiakas, D.1    Raina, S.2
  • 23
    • 0031055372 scopus 로고    scopus 로고
    • Evidence for PDZ domains in bacteria, yeast, and plants
    • Ponting, C.P. (1997) Evidence for PDZ domains in bacteria, yeast, and plants. Protein Sci 6: 464-468.
    • (1997) Protein Sci , vol.6 , pp. 464-468
    • Ponting, C.P.1
  • 24
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: Targeting signalling molecules to sub-membranous sites
    • Ponting, C.P., Phillips, C., Davies, K.E., and Blake, D.J. (1997) PDZ domains: targeting signalling molecules to sub-membranous sites. Bioessays 19: 469-479.
    • (1997) Bioessays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 25
    • 0037118622 scopus 로고    scopus 로고
    • Phage HK022-based integrative vectors for the insertion of genes in the chromosome of multiply marked Escherichia coli strains
    • Rossignol, M., Moulin, L., and Boccard, F. (2002) Phage HK022-based integrative vectors for the insertion of genes in the chromosome of multiply marked Escherichia coli strains. FEMS Microbiol Lett 213: 45-49.
    • (2002) FEMS Microbiol Lett , vol.213 , pp. 45-49
    • Rossignol, M.1    Moulin, L.2    Boccard, F.3
  • 26
    • 0033593022 scopus 로고    scopus 로고
    • A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors
    • Rudner, D.Z., Fawcett, P., and Losick, R. (1999) A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors. Proc Natl Acad Sci USA 96: 14765-14770.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14765-14770
    • Rudner, D.Z.1    Fawcett, P.2    Losick, R.3
  • 28
    • 0032805531 scopus 로고    scopus 로고
    • PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease
    • Sassoon, N., Arie, J.P., and Betton, J.M. (1999) PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease. Mol Microbiol 33: 583-589.
    • (1999) Mol Microbiol , vol.33 , pp. 583-589
    • Sassoon, N.1    Arie, J.P.2    Betton, J.M.3
  • 29
    • 0037131258 scopus 로고    scopus 로고
    • PDZ domains facilitate binding of high temperature requirement protease A (HtrA) and tailspecific protease (Tsp) to heterologous substrates through recognition of the small stable RNA A (ssrA)-encoded peptide
    • Spiers, A., Lamb, H.K., Cocklin, S., Wheeler, K.A., Budworth, J., Dodds, A.L., et al. (2002) PDZ domains facilitate binding of high temperature requirement protease A (HtrA) and tailspecific protease (Tsp) to heterologous substrates through recognition of the small stable RNA A (ssrA)-encoded peptide. J Biol Chem 277: 39443-39449.
    • (2002) J Biol Chem , vol.277 , pp. 39443-39449
    • Spiers, A.1    Lamb, H.K.2    Cocklin, S.3    Wheeler, K.A.4    Budworth, J.5    Dodds, A.L.6
  • 30
    • 0036777494 scopus 로고    scopus 로고
    • Intramembrane proteolysis controls diverse signalling pathways throughout evolution
    • Urban, S., and Freeman, M. (2002) Intramembrane proteolysis controls diverse signalling pathways throughout evolution. Curr Opin Genet Dev 12: 512-518.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 512-518
    • Urban, S.1    Freeman, M.2
  • 31
    • 0030066650 scopus 로고    scopus 로고
    • Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease
    • Waller, P.R., and Sauer, R.T. (1996) Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J Bacteriol 178: 1146-1153.
    • (1996) J Bacteriol , vol.178 , pp. 1146-1153
    • Waller, P.R.1    Sauer, R.T.2
  • 32
    • 0344953579 scopus 로고    scopus 로고
    • OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
    • Walsh, N.P., Alba, B.M., Bose, B., Gross, C.A., and Sauer, R.T. (2003) OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell 113: 61-71.
    • (2003) Cell , vol.113 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.