메뉴 건너뛰기




Volumn 5, Issue 5, 2009, Pages

Intrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHIMERIC PROTEIN; ENDOPEPTIDASE LA; ROVA PROTEIN; UNCLASSIFIED DRUG; ROVA PROTEIN, YERSINIA; TRANSCRIPTION FACTOR;

EID: 67249097456     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1000435     Document Type: Article
Times cited : (81)

References (53)
  • 1
    • 0034056597 scopus 로고    scopus 로고
    • Temperature-regulated expression of bacterial virulence genes
    • DOI 10.1016/S1286-4579(00)00272-0
    • Konkel ME, Tilly K (2000) Temperature-regulated expression of bacterial virulence genes. Microbes Infect 2: 157-166. (Pubitemid 30154705)
    • (2000) Microbes and Infection , vol.2 , Issue.2 , pp. 157-166
    • Konkel, M.E.1    Tilly, K.2
  • 2
    • 34248147423 scopus 로고    scopus 로고
    • Thermosensors in eubacteria: Role and evolution
    • DOI 10.1007/s12038-007-0054-8
    • Schumann W (2007) Thermosensors in eubacteria: role and evolution. J Biosci 32: 549-557. (Pubitemid 46708705)
    • (2007) Journal of Biosciences , vol.32 , Issue.3 , pp. 549-557
    • Schumann, W.1
  • 3
    • 0029134671 scopus 로고
    • Environmental modulation of gene expression and pathogenesis in Yersinia
    • Straley SC, Perry RD (1995) Environmental modulation of gene expression and pathogenesis in Yersinia. Trends Microbiol 3: 310-317.
    • (1995) Trends Microbiol , vol.3 , pp. 310-317
    • Straley, S.C.1    Perry, R.D.2
  • 5
    • 0031002852 scopus 로고    scopus 로고
    • Yersinia enterocolitica: The charisma continues
    • Bottone EJ (1997) Yersinia enterocolitica: the charisma continues. Clin Microbiol Rev 10: 257-276. (Pubitemid 27196671)
    • (1997) Clinical Microbiology Reviews , vol.10 , Issue.2 , pp. 257-276
    • Bottone, E.J.1
  • 7
    • 22944479296 scopus 로고    scopus 로고
    • Transcriptional regulation in Yersinia: An update
    • Marceau M (2005) Transcriptional regulation in Yersinia: an update. Curr Issues Mol Biol 7: 151-177.
    • (2005) Curr Issues Mol Biol , vol.7 , pp. 151-177
    • Marceau, M.1
  • 9
    • 0020073144 scopus 로고
    • Temperature-inducible outer membrane protein of Yersinia pseudotuberculosis and Yersinia enterocolitica is associated with the virulence plasmid
    • Bolin I, Norlander I, Wolf-Watz H (1982) Temperature-inducible outer membrane protein of Yersinia pseudotuberculosis and Yersinia enterocolitica is associated with the virulence plasmid. Infect Immun 37: 506-512.
    • (1982) Infect Immun , vol.37 , pp. 506-512
    • Bolin, I.1    Norlander, I.2    Wolf-Watz, H.3
  • 10
    • 0032803976 scopus 로고    scopus 로고
    • The Yersinia enterocolitica pYV virulence plasmid contains multiple intrinsic DNA bends which melt at 37°C
    • Rohde JR, Luan XS, Rohde H, Fox JM, Minnich SA (1999) The Yersinia enterocolitica pYV virulence plasmid contains multiple intrinsic DNA bends which melt at 37 degrees C. J Bacteriol 181: 4198-4204. (Pubitemid 29331376)
    • (1999) Journal of Bacteriology , vol.181 , Issue.14 , pp. 4198-4204
    • Rohde, J.R.1    Luan, X.-S.2    Rohde, H.3    Fox, J.M.4    Minnich, S.A.5
  • 11
    • 9644301279 scopus 로고    scopus 로고
    • The ATP-dependent ClpXP and Lon proteases regulate expression of the Yersinia pestis type III secretion system via regulated proteolysis of YmoA, a small histone-like protein
    • DOI 10.1111/j.1365-2958.2004.04353.x
    • Jackson MW, Silva-Herzog E, Plano GV (2004) The ATP-dependent ClpXP and Lon proteases regulate expression of the Yersinia pestis type III secretion system via regulated proteolysis of YmoA, a small histone-like protein. Mol Microbiol 54: 1364-1378. (Pubitemid 39578278)
    • (2004) Molecular Microbiology , vol.54 , Issue.5 , pp. 1364-1378
    • Jackson, M.W.1    Silva-Herzog, E.2    Plano, G.V.3
  • 12
    • 0027141070 scopus 로고
    • Temperature sensing in Yersinia pestis: Translation of the LcrF activator protein is thermally regulated
    • Hoe NP, Goguen JD (1993) Temperature sensing in Yersinia pestis: translation of the LcrF activator protein is thermally regulated. J Bacteriol 175: 7901-7909. (Pubitemid 24004397)
    • (1993) Journal of Bacteriology , vol.175 , Issue.24 , pp. 7901-7909
    • Hoe, N.P.1    Goguen, J.D.2
  • 13
    • 0030668089 scopus 로고    scopus 로고
    • The Rap and Hor proteins of Erwinia, Serratia and Yersinia: A novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens
    • Thomson NR, Cox A, Bycroft BW, Stewart GS, Williams P, et al. (1997) The Rap and Hor proteins of Erwinia, Serratia and Yersinia: a novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens. Mol Microbiol 26: 531-544.
    • (1997) Mol Microbiol , vol.26 , pp. 531-544
    • Thomson, N.R.1    Cox, A.2    Bycroft, B.W.3    Stewart, G.S.4    Williams, P.5
  • 14
    • 33645858540 scopus 로고    scopus 로고
    • Regulation of virulence by members of the MarR/SlyA family
    • Ellison DW, Miller VL (2006) Regulation of virulence by members of the MarR/SlyA family. Curr Opin Microbiol 9: 153-159.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 153-159
    • Ellison, D.W.1    Miller, V.L.2
  • 15
    • 84934440556 scopus 로고    scopus 로고
    • Regulatory elements implicated in the environmental control of invasin expression in enteropathogenic Yersinia
    • Heroven AK, Böhme K, Tran-Winkler H, Dersch P (2007) Regulatory elements implicated in the environmental control of invasin expression in enteropathogenic Yersinia. Adv Exp Med Biol 603: 156-166.
    • (2007) Adv Exp Med Biol , vol.603 , pp. 156-166
    • Heroven, A.K.1    Böhme, K.2    Tran-Winkler, H.3    Dersch, P.4
  • 16
    • 0033975434 scopus 로고    scopus 로고
    • A chromosomally encoded regulator is required for expression of the Yersinia enterocolitica inv gene and for virulence
    • DOI 10.1046/j.1365-2958.2000.01740.x
    • Revell PA, Miller VL (2000) A chromosomally encoded regulator is required for expression of the Yersinia enterocolitica inv gene and for virulence. Mol Microbiol 35: 677-685. (Pubitemid 30085284)
    • (2000) Molecular Microbiology , vol.35 , Issue.3 , pp. 677-685
    • Revell, P.A.1    Miller, V.L.2
  • 17
    • 0034797422 scopus 로고    scopus 로고
    • Environmental control of invasin expression in Yersinia pseudotuberculosis is mediated by regulation of RovA, a transcriptional activator of the SlyA/Hor family
    • DOI 10.1046/j.1365-2958.2001.02522.x
    • Nagel G, Lahrz A, Dersch P (2001) Environmental control of invasin expression in Yersinia pseudotuberculosis is mediated by regulation of RovA, a transcriptional activator of the SlyA/Hor family. Mol Microbiol 41: 1249-1269. (Pubitemid 32939499)
    • (2001) Molecular Microbiology , vol.41 , Issue.6 , pp. 1249-1269
    • Nagel, G.1    Lahrz, A.2    Dersch, P.3
  • 18
    • 33750695273 scopus 로고    scopus 로고
    • RovM, a novel LysR-type regulator of the virulence activator gene rovA, controls cell invasion, virulence and motility of Yersinia pseudotuberculosis
    • DOI 10.1111/j.1365-2958.2006.05458.x
    • Heroven AK, Dersch P (2006) RovM, a novel LysR-type regulator of the virulence activator gene rovA, controls cell invasion, virulence and motility of Yersinia pseudotuberculosis. Mol Microbiol 62: 1469-1483. (Pubitemid 44707207)
    • (2006) Molecular Microbiology , vol.62 , Issue.5 , pp. 1469-1483
    • Heroven, A.K.1    Dersch, P.2
  • 20
    • 3843113478 scopus 로고    scopus 로고
    • RovA is autoregulated and antagonizes H-NS-mediated silencing of invasin and rovA expression in Yersinia pseudotuberculosis
    • DOI 10.1111/j.1365-2958.2004.04162.x
    • Heroven AK, Nagel G, Tran HJ, Parr S, Dersch P (2004) RovA is autoregulated and antagonizes H-NS-mediated silencing of invasin and rovA expression in Yersinia pseudotuberculosis. Mol Microbiol 53: 871-888. (Pubitemid 39036966)
    • (2004) Molecular Microbiology , vol.53 , Issue.3 , pp. 871-888
    • Heroven, A.K.1    Nagel, G.2    Tran, H.J.3    Parr, S.4    Dersch, P.5
  • 21
    • 34547764310 scopus 로고    scopus 로고
    • Comparative analysis of the regulation of rovA from the pathogenic yersiniae
    • DOI 10.1128/JB.00528-07
    • Lawrenz MB, Miller VL (2007) Comparative analysis of the regulation of rovA from the pathogenic yersiniae. J Bacteriol 189: 5963-5975. (Pubitemid 47236149)
    • (2007) Journal of Bacteriology , vol.189 , Issue.16 , pp. 5963-5975
    • Lawrenz, M.B.1    Miller, V.L.2
  • 22
    • 33745889008 scopus 로고    scopus 로고
    • H-NS represses inv transcription in Yersinia enterocolitica through competition with RovA and interaction with YmoA
    • DOI 10.1128/JB.00862-05
    • Ellison DW, Miller VL (2006) H-NS represses inv transcription in Yersinia enterocolitica through competition with RovA and interaction with YmoA. J Bacteriol 188: 5101-5112. (Pubitemid 44051476)
    • (2006) Journal of Bacteriology , vol.188 , Issue.14 , pp. 5101-5112
    • Ellison, D.W.1    Miller, V.L.2
  • 23
    • 29644440330 scopus 로고    scopus 로고
    • Analysis of RovA, a transcriptional regulator of Yersinia pseudotuberculosis virulence that acts through antirepression and direct transcriptional activation
    • DOI 10.1074/jbc.M504464200
    • Tran HJ, Heroven AK, Winkler L, Spreter T, Beatrix B, et al. (2005) Analysis of RovA, a transcriptional regulator of Yersinia pseudotuberculosis virulence that acts through antirepression and direct transcriptional activation. J Biol Chem 280: 42423-42432. (Pubitemid 43023215)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.51 , pp. 42423-42432
    • Tran, H.J.1    Heroven, A.K.2    Winkler, L.3    Spreter, T.4    Beatrix, B.5    Dersch, P.6
  • 24
    • 43449103621 scopus 로고    scopus 로고
    • A Csr-type regulatory system, including small non-coding RNAs, regulates the global virulence regulator RovA of Yersinia pseudotuberculosis through RovM
    • DOI 10.1111/j.1365-2958.2008.06218.x
    • Heroven AK, Böhme K, Rohde M, Dersch P (2008) A Csr-type regulatory system, including small non-coding RNAs, regulates the global virulence regulator RovA of Yersinia pseudotuberculosis through RovM. Mol Microbiol 68: 1179-1195. (Pubitemid 351670194)
    • (2008) Molecular Microbiology , vol.68 , Issue.5 , pp. 1179-1195
    • Heroven, A.K.1    Bohme, K.2    Rohde, M.3    Dersch, P.4
  • 25
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • DOI 10.1016/0968-0004(96)10052-9
    • Lupas A (1996) Coiled coils: new structures and new functions. Trends Biochem Sci 21: 375-382. (Pubitemid 26338674)
    • (1996) Trends in Biochemical Sciences , vol.21 , Issue.10 , pp. 375-382
    • Lupas, A.1
  • 26
    • 0025044578 scopus 로고
    • Carboxy-terminal determinants of intracellular protein degradation
    • Parsell DA, Silber KR, Sauer RT (1990) Carboxy-terminal determinants of intracellular protein degradation. Genes Dev 4: 277-286. (Pubitemid 20062754)
    • (1990) Genes and Development , vol.4 , Issue.2 , pp. 277-286
    • Parsell, D.A.1    Silber, K.R.2    Sauer, R.T.3
  • 27
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler KC, Waller PR, Sauer RT (1996) Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271: 990-993. (Pubitemid 26066397)
    • (1996) Science , vol.271 , Issue.5251 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.H.2    Sauer, R.T.3
  • 28
    • 0032841896 scopus 로고    scopus 로고
    • A mutant HemA protein with positive charge close to the N terminus is stabilized against heme-regulated proteolysis in Salmonella typhimurium
    • Wang L, Wilson S, Elliott T (1999) A mutant HemA protein with positive charge close to the N terminus is stabilized against heme-regulated proteolysis in Salmonella typhimurium. J Bacteriol 181: 6033-6041. (Pubitemid 29459914)
    • (1999) Journal of Bacteriology , vol.181 , Issue.19 , pp. 6033-6041
    • Wang, L.1    Wilson, S.2    Elliott, T.3
  • 29
    • 54049111071 scopus 로고    scopus 로고
    • Tuning the strength of a bacterial N-end rule degradation signal
    • Wang KH, Oakes ES, Sauer RT, Baker TA (2008) Tuning the strength of a bacterial N-end rule degradation signal. J Biol Chem 283: 24600-24607.
    • (2008) J Biol Chem , vol.283 , pp. 24600-24607
    • Wang, K.H.1    Oakes, E.S.2    Sauer, R.T.3    Baker, T.A.4
  • 30
    • 0032535038 scopus 로고    scopus 로고
    • Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: In vitro degradation and identification of residues required for proteolysis
    • Gonzalez M, Frank EG, Levine AS, Woodgate R (1998) Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis. Genes Dev 12: 3889-3899. (Pubitemid 29024851)
    • (1998) Genes and Development , vol.12 , Issue.24 , pp. 3889-3899
    • Gonzalez, M.1    Frank, E.G.2    Levine, A.S.3    Woodgate, R.4
  • 31
    • 41949134709 scopus 로고    scopus 로고
    • Functional mechanics of the ATP-dependent Lon protease - Lessons from endogenous protein and synthetic peptide substrates
    • Lee I, Suzuki CK (2008) Functional mechanics of the ATP-dependent Lon protease - lessons from endogenous protein and synthetic peptide substrates. Biochim Biophys Acta 1784: 727-735.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 727-735
    • Lee, I.1    Suzuki, C.K.2
  • 33
    • 0026503828 scopus 로고
    • The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
    • Goldberg AL (1992) The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur J Biochem 203: 9-23.
    • (1992) Eur J Biochem , vol.203 , pp. 9-23
    • Goldberg, A.L.1
  • 34
    • 33748131674 scopus 로고    scopus 로고
    • The temperature-sensing protein TlpA is repressed by PhoP and dispensable for virulence of Salmonella enterica serovar Typhimurium in mice
    • DOI 10.1016/j.micinf.2006.04.015, PII S128645790600181X
    • Gal-Mor O, Valdez Y, Finlay BB (2006) The temperature-sensing protein TlpA is repressed by PhoP and dispensable for virulence of Salmonella enterica serovar Typhimurium in mice. Microbes Infect 8: 2154-2162. (Pubitemid 44311592)
    • (2006) Microbes and Infection , vol.8 , Issue.8 , pp. 2154-2162
    • Gal-Mor, O.1    Valdez, Y.2    Finlay, B.B.3
  • 35
    • 0031472233 scopus 로고    scopus 로고
    • A proteinaceous gene regulatory thermometer in Salmonella
    • DOI 10.1016/S0092-8674(00)80313-X
    • Hurme R, Berndt KD, Normark SJ, Rhen M (1997) A proteinaceous gene regulatory thermometer in Salmonella. Cell 90: 55-64. (Pubitemid 28009418)
    • (1997) Cell , vol.90 , Issue.1 , pp. 55-64
    • Hurme, R.1    Berndt, K.D.2    Normark, S.J.3    Rhen, M.4
  • 37
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in Bacterial Regulatory Circuits
    • DOI 10.1146/annurev.cellbio.19.110701.153228
    • Gottesman S (2003) Proteolysis in bacterial regulatory circuits. Annu Rev Cell Dev Biol 19: 565-587. (Pubitemid 37487361)
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 38
    • 41149142931 scopus 로고    scopus 로고
    • Resolving individual steps in the operation of ATPdependent proteolytic molecular machines: From conformational changes to substrate translocation and processivity
    • Licht S, Lee I (2008) Resolving individual steps in the operation of ATPdependent proteolytic molecular machines: from conformational changes to substrate translocation and processivity. Biochemistry 47: 3595-3605.
    • (2008) Biochemistry , vol.47 , pp. 3595-3605
    • Licht, S.1    Lee, I.2
  • 40
    • 33748703166 scopus 로고    scopus 로고
    • Biological roles of the Lon ATP-dependent protease
    • DOI 10.1016/j.resmic.2006.05.004, PII S0923250806001239
    • Tsilibaris V, Maenhaut-Michel G, Van Melderen L (2006) Biological roles of the Lon ATP-dependent protease. Res Microbiol 157: 701-713. (Pubitemid 44389733)
    • (2006) Research in Microbiology , vol.157 , Issue.8 , pp. 701-713
    • Tsilibaris, V.1    Maenhaut-Michel, G.2    Van Melderen, L.3
  • 41
    • 31344443334 scopus 로고    scopus 로고
    • Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins
    • Wilkinson SP, Grove A (2006) Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins. Curr Issues Mol Biol 8: 51-62. (Pubitemid 43141390)
    • (2006) Current Issues in Molecular Biology , vol.8 , Issue.1 , pp. 51-62
    • Wilkinson, S.P.1    Grove, A.2
  • 42
    • 58549088127 scopus 로고    scopus 로고
    • A dual-signal regulatory circuit activates transcription of a set of divergent operons in Salmonella typhimurium
    • Zhao G, Weatherspoon N, Kong W, Curtiss R 3rd, Shi Y (2008) A dual-signal regulatory circuit activates transcription of a set of divergent operons in Salmonella typhimurium. Proc Natl Acad Sci U S A 105: 20924-20929.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20924-20929
    • Zhao, G.1    Weatherspoon, N.2    Kong, W.3    Curtiss III, R.4    Shi, Y.5
  • 43
    • 33751228400 scopus 로고    scopus 로고
    • ATP-dependent proteases of bacteria: Recognition logic and operating principles
    • DOI 10.1016/j.tibs.2006.10.006, PII S0968000406002969
    • Baker TA, Sauer RT (2006) ATP-dependent proteases of bacteria: recognition logic and operating principles. Trends Biochem Sci 31: 647-653. (Pubitemid 44791948)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.12 , pp. 647-653
    • Baker, T.A.1    Sauer, R.T.2
  • 44
    • 50049083221 scopus 로고    scopus 로고
    • Recognition of misfolded proteins by Lon, a AAA+ protease
    • Gur E, Sauer RT (2008) Recognition of misfolded proteins by Lon, a AAA+ protease. Genes Dev 22: 2267-2277.
    • (2008) Genes Dev , vol.22 , pp. 2267-2277
    • Gur, E.1    Sauer, R.T.2
  • 45
    • 33644935094 scopus 로고    scopus 로고
    • 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
    • Shah IM, Wolf RE 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.
    • (2006) J Mol Biol , vol.357 , pp. 718-731
    • Shah, I.M.1    Wolf Jr., R.E.2
  • 46
    • 33644839119 scopus 로고    scopus 로고
    • Inhibition of Lon-dependent degradation of the Escherichia coli transcription activator SoxS by interaction with 'soxbox' DNA or RNA polymerase
    • Shah IM, Wolf RE 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.
    • (2006) Mol Microbiol , vol.60 , pp. 199-208
    • Shah, I.M.1    Wolf Jr., R.E.2
  • 47
    • 0032540286 scopus 로고    scopus 로고
    • NMR structure of the bacteriophage λ N peptide/boxB RNA complex: Recognition of a GNRA fold by an arginine-rich motif
    • DOI 10.1016/S0092-8674(00)81579-2
    • Legault P, Li J, Mogridge J, Kay LE, Greenblatt J (1998) NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif. Cell 93: 289-299. (Pubitemid 28180861)
    • (1998) Cell , vol.93 , Issue.2 , pp. 289-299
    • Legault, P.1    Li, J.2    Mogridge, J.3    Kay, L.E.4    Greenblatt, J.5
  • 48
    • 0035830914 scopus 로고    scopus 로고
    • The Molecular Chaperone DnaJ Is Required for the Degradation of a Soluble Abnormal Protein in Escherichia coli
    • DOI 10.1074/jbc.M002937200
    • Huang HC, Sherman MY, Kandror O, Goldberg AL (2001) The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli. J Biol Chem 276: 3920-3928. (Pubitemid 37371471)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.6 , pp. 3920-3928
    • Huang, H.-C.1    Sherman, M.Y.2    Kandror, O.3    Goldberg, A.L.4
  • 49
    • 4444377383 scopus 로고    scopus 로고
    • Modulating substrate choice: The SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation
    • DOI 10.1101/gad.1240104
    • Flynn JM, Levchenko I, Sauer RT, Baker TA (2004) Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation. Genes Dev 18: 2292-2301. (Pubitemid 39209577)
    • (2004) Genes and Development , vol.18 , Issue.18 , pp. 2292-2301
    • Flynn, J.M.1    Levchenko, I.2    Sauer, R.T.3    Baker, T.A.4
  • 50
    • 0033820028 scopus 로고    scopus 로고
    • Polypeptide stimulators of the Ms-Lon protease
    • Rudyak SG, Shrader TE (2000) Polypeptide stimulators of the Ms-Lon protease. Protein Sci 9: 1810-1817. (Pubitemid 30745477)
    • (2000) Protein Science , vol.9 , Issue.9 , pp. 1810-1817
    • Rudyak, S.G.1    Shrader, T.E.2
  • 51
    • 4544343195 scopus 로고    scopus 로고
    • Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli
    • DOI 10.1074/jbc.M404725200
    • Nomura K, Kato J, Takiguchi N, Ohtake H, Kuroda A (2004) Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli. J Biol Chem 279: 34406-34410. (Pubitemid 39318066)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34406-34410
    • Nomura, K.1    Kato, J.2    Takiguchi, N.3    Ohtake, H.4    Kuroda, A.5
  • 52
    • 34247844506 scopus 로고    scopus 로고
    • Ligand-controlled proteolysis of the Escherichia coli transcriptional regulator ZntR
    • DOI 10.1128/JB.01531-06
    • Pruteanu M, Neher SB, Baker TA (2007) Ligand-controlled proteolysis of the Escherichia coli transcriptional regulator ZntR. J Bacteriol 189: 3017-3025. (Pubitemid 46697390)
    • (2007) Journal of Bacteriology , vol.189 , Issue.8 , pp. 3017-3025
    • Pruteanu, M.1    Neher, S.B.2    Baker, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.