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Roles for Energy-Dependent Proteases in Regulatory Cascades

  • Chapter
Regulation of Gene Expression in Escherichia coli

Abstract

In theory, the rapid degradation of a protein may play as critical a role in regulating protein activity as controls on transcription and translation. However, the role of protein turnover in regulation received relatively little attention during the years when the elegant systems for regulation of transcription initiation were first being investigated. The first dramatic example of a proteolytic event with clear regulatory consequences was provided by the demonstration, in 1975, that induction of bacteriophage lambda after DNA damage was due to cleavage of the lambda repressor.1 Since those experiments, an increasing number of proteases and interesting protein targets have been identified, both in prokaryotes and eukaryotes.

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References

  1. Roberts JW, Roberts CW. Proteolytic cleavage of bacteriophage lambda repressor in induction. Proc Natl Acad Sci USA 1975; 72:147–151.

    Google Scholar 

  2. Goldberg AL. Degradation of abnormal proteins in Escherichia coli. Proc Natl Acad Sci 1972; 69:422–426.

    Google Scholar 

  3. Goldberg AL, John ACS. Intracellular protein degradation in mammalian and bacterial cells. Annu Rev Biochem 1976; 45:747–803.

    Google Scholar 

  4. Hershko A, Ciechanover A. The Ubiquitin system for protein degradation. Annu Rev Biochem 1992; 61:761–807.

    Google Scholar 

  5. Gottesman S, Maurizi MR. Regulation by proteolysis: Energy-dependent proteases and their targets. Microbiol Rev 1992; 56:592–621.

    Google Scholar 

  6. Maurizi MR. Proteases and protein degradation in Escherichia coli. Experientia 1992; 48:178–201.

    Google Scholar 

  7. Konrad MW. Dependence of ‘early’ λ bacteriophage RNA synthesis on bacteriophage-directed protein synthesis. Proc Natl Acad Sci USA 1968; 59:171–178.

    Google Scholar 

  8. Schwartz M. On the function of the N cistron in phage λ. Virology 1970; 40:23–33.

    Google Scholar 

  9. Weisberg RA, Gottesman ME. The stability of Int and Xis functions. In: Hershey AD, ed. The Bacteriophage Lambda. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1971:489–500

    Google Scholar 

  10. Wyatt WM, Inokuchi H. Stability of lambda O and P replication functions. Virology 1974; 58:313–315.

    Google Scholar 

  11. Belfort M, Wulff D. The roles of the lambda cIII gene and the Escherichia coli catabolite gene activation system in the establishment of lysogeny by bacteriophage lambda. Proc Natl Acad Sci USA 1974; 71:779–782.

    Google Scholar 

  12. Reichardt LF. Control of bacteriophage lambda repressor synthesis after phage infection: the role of the N, cII, cIII and cro products. J Mol Biol 1975; 93:267–288.

    Google Scholar 

  13. Jones MO, Herskowitz I. Mutants of bacteriophage λ which do not require the cIII gene for efficient lysogenization. Virology 1978; 88:199–212.

    Google Scholar 

  14. Roberts JW, Roberts CW, Mount DW. Inactivation and proteolytic cleavage of phage λ repressor in vitro in an ATP-dependent reaction. Proc Natl Acad Sci USA 1977; 74:2283–2287.

    Google Scholar 

  15. Roberts JW, Roberts CW, Craig NL. Escherichia coli recA gene product inactivates phage λ repressor. Proc Natl Acad Sci USA 1978; 75:4714–4718.

    Google Scholar 

  16. Roberts JW, Devoret R. Lysogenic Induction. In: Hendrix RW, Roberts JW, Stahl FW, Weisberg RA, eds. Lambda II. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1983:123–144

    Google Scholar 

  17. Little JW, Edmiston SH, Pacelli LZ et al. Cleavage of the Escherichia coli lexA protein by the recA protease. Proc Natl Acad Sci USA 1980; 77:3225–3229.

    Google Scholar 

  18. Nohmi T, Battista JR, Dodson LA et al. RecA-mediated cleavage activates UmuD for mutagenesis: Mechanistic relationship between transcriptional derepression and posttranslational activation. Proc Natl Acad Sci USA 1988; 85:1816–1820.

    Google Scholar 

  19. Slilaty SN, Little JW. Lysine-156 and serine-119 are required for LexA repressor cleavage: a possible mechanism. Proc Natl Acad Sci USA 1987; 84:3987–3991.

    Google Scholar 

  20. Little JW. Mechanism of specific LexA cleavage: autodigestion and the role of RecA coprotease. Biochimie 1991; 73:411–422.

    Google Scholar 

  21. Little JW. Autodigestion of LexA and phage lambda repressors. Proc Natl Acad Sci USA 1984; 81:1375–1379.

    Google Scholar 

  22. Craig NL, Roberts JW. E. coli recA protein-directed cleavage of phage λ repressor requires polynucleotide. Nature 1980; 283:26–30.

    Google Scholar 

  23. Little JW. LexA cleavage and other self-processing reactions. J Bacteriol 1993; 175:4943–4950.

    Google Scholar 

  24. Howard-Flanders P, Simson E, Theriot L. A locus that controls filament formation and sensitivity to radiation in Escherichia coli K12. Genetics 1964; 49:237–246.

    Google Scholar 

  25. Markovitz A. Regulatory mechanisms for synthesis of capsular polysaccharide in mucoid mutants of Escherichia coli K12. Proc Natl Acad Sci USA 1964; 51:239–246.

    Google Scholar 

  26. Bukhari AI, Zipser D. Mutants of Escherichia coli with a defect in the degradation of nonsense fragments. Nature 1973; 243:238–241.

    Google Scholar 

  27. Gottesman S, Zipser D. Deg phenotype of Escherichia coli lon mutants. J Bacteriol 1978; 113:844–851.

    Google Scholar 

  28. Charette M, Henderson GW, Markovitz A. ATP hydrolysis- dependent activity of the lon(capR) protein of E. coli K12. Proc Natl Acad Sci USA 1981; 78:4728–4732.

    Google Scholar 

  29. Chung CH, Goldberg AL. The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Proc Natl Acad Sci USA 1981; 78:4931–4935.

    Google Scholar 

  30. Grossman AD, Burgess R, Walter W et al. Mutations in the lon gene of E. coli K12 phenotypically suppress a mutation in the a subunit of RNA polymerase. Cell 1983; 32:151–159.

    Google Scholar 

  31. Gottesman S, Gottesman ME, Shaw JE et al. Protein degradation in E. coli: the lon mutation and bacteriophage lambda N and cII protein stability. Cell 1981; 24:225–233.

    Google Scholar 

  32. Maurizi MR. Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli. J Biol Chem 1987; 262:2696–2703.

    Google Scholar 

  33. George J, Castellazzi M, Buttin G. Prophage induction and cell division in E. coli. III. Mutations sfiA and sfiB restore division in tif and lon strains and permit the mutator properties of tif. Mol Gen Genet 1975; 140:309–332.

    Google Scholar 

  34. Castellazi M, George J, Buttin G. Prophage induction and cell division in E. coli. I. Further characterization of the thermosensitive mutation tif-1 whose expression mimics the effect of UV irradiation. Mol Gen Genet 1972; 119:139–152.

    Google Scholar 

  35. Gottesman S, Halpern E, Trisler P. Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12. J Bacteriol 1981; 148:265–273.

    Google Scholar 

  36. Huisman O, D’Ari R, George J. Further characterization of sfiA and sfiB mutations in Escherichia coli. J Bacteriol 1980; 144:185 – 191.

    Google Scholar 

  37. Gayda RC, Yamamoto LT, Markovitz A. Second-site mutations in capR (lon) strains of Escherichia coli K-12 that prevent radiation sensitivity and allow bacteriophage lambda to lysogenize. J Bacteriol 1976; 127:1208–1216.

    Google Scholar 

  38. Johnson BF. Fine structure mapping and properties of mutations suppressing the lon mutation in Escherichia coli K12 and B strains. Genet Res 1977; 30:273–286.

    Google Scholar 

  39. Johnson BF, Greenberg J. Mapping of sul, the suppressor of lon in Escherichia coli. J Bacteriol 1975; 122:570–574.

    Google Scholar 

  40. Huisman O, D’Ari R, Gottesman S. Cell division control in Escherichia coli: specific induction of the SOS SfiA protein is sufficient to block septation. Proc Natl Acad Sci USA 1984; 81:4490–4494.

    Google Scholar 

  41. Mizusawa S, Gottesman S. Protein degradation in Escherichia coli: the lon gene controls the stability of the SulA protein. Proc. Natl Acad Sci USA 1983; 80:358–362.

    Google Scholar 

  42. Schoemaker JM, Gayda RC, Markovitz A. Regulation of cell division in Escherichia coli: SOS induction and cellular location of the SulA protein, a key to lon-associated filamentation and death. J Bacteriol 1984; 158:551–561.

    Google Scholar 

  43. Mizusawa S, Court D, Gottesman S. Transcription of the sulA gene and repression by LexA. J Mol Biol 1983; 171:337–343.

    Google Scholar 

  44. Huisman O, D’Ari R. An inducible DNA-replication-cell division coupling mechanism in E. coli. Nature 1981; 290:797–799.

    Google Scholar 

  45. Lutkenhaus JF. Coupling of DNA replication and cell divison: sulB is an allele of fisZ. J Bacteriol 1983; 154:1339–1346.

    Google Scholar 

  46. Maguin E, Lutkenhaus J, D’Ari R. Reversibility of SOS-associated division inhibition in Escherichia coli. J Bacteriol 1986; 166:733–738.

    Google Scholar 

  47. Jones C, Holland IB. Role of the SulB (FtsZ) protein in division inhibition during the SOS response in Escherichia coli: FtsZ stabilizes the inhibitor SulA in maxicells. Proc Natl Acad Sci USA 1985; 82:6045–6049.

    Google Scholar 

  48. Casadaban MJ, Cohen SN. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences. Proc Natl Acad Sci USA 1979; 76:4530–4533.

    Google Scholar 

  49. Markovitz A. Genetics and regulation of bacterial capsular polysaccharide biosynthesis and radiation sensitivity. In: Sutherland I, ed. Surface Carbohydrates of the Prokaryotic Cell. London: Academic Press, 1977:415–462

    Google Scholar 

  50. Trisler P, Gottesman S. lon transcriptional regulation of genes necessary for capsular polysaccharide synthesis in Escherichia coli K-12. J Bacteriol 1984; 160:184–191.

    Google Scholar 

  51. Gottesman S, Trisler P, Torres-Cabassa AS. Regulation of capsular polysaccharide synthesis in Escherichia coli K12: characterization of three regulatory genes. J Bacteriol 1985; 62:1111–1119.

    Google Scholar 

  52. Torres-Cabassa AS, Gottesman S. Capsule synthesis in Escherichia coli K-12 is regulated by proteolysis. J Bacteriol 1987; 169:981–989.

    Google Scholar 

  53. Stout V, Torres-Cabassa A, Maurizi MR et al. RcsA, an unstable positive regulator of capsular polysaccharide synthesis. J Bacteriol 1991; 173:1738–1747.

    Google Scholar 

  54. Sledjeski D, Gottesman S. A small RNA acts as an antisilenceer of the H-NS-silenced rcsA gene of Escherichia coli. Proc Natl Acad Sci USA 1995; 92:2003–2007.

    Google Scholar 

  55. Gottesman S. Regulation of Capsule Synthesis: Modification of the two-component paradigm by an accessory unstable regulator. In: Hoch JA, Silhavy TJ, eds. Signal Transduction in Bacteria. Washington, DC: American Society for Microbiology, 1995:253–262

    Google Scholar 

  56. Snyder WB, Silhavy TJ. Enchanced export of β-galactosidase fusion proteins in prlF mutants is Lon dependent. J Bacteriol 1992; 174:5661.

    Google Scholar 

  57. Lam H-M, Tancula E, Dempsey WB et al. Suppression of insertions in the complex pdxJ Operon of Escherichia coli K-12 by lon and other mutations. J Bacteriol 1992; 174:1554–1567.

    Google Scholar 

  58. Yarmolinsky M. Programmed Cell Death in Bacterial Populations. Science 1995; 267:836–837.

    Google Scholar 

  59. Tsuchimoto S, Nishimura Y, Ohtsubo E. The stable maintenance system pern of plasmid R100: Degradation of PemI protein may allow PemK protein to inhibit cell growth. J Bacteriol 1992; 174:4205–4211.

    Google Scholar 

  60. Van Melderen L, Bernard P, Couturier M. Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria. Molec Microbiol 1994; 11:1151–1157.

    Google Scholar 

  61. Tojo N, Inouye S, Komano T. Cloning and nucleotide sequence of the Myxococcus xanthus lon gene: indispensability of lon for vegetative growth. J Bacteriol 1993; 175:2271–2277.

    Google Scholar 

  62. Tojo N, Inouye S, Komano T. The lonD gene is homologous to the lon gene encoding an ATP-dependent protease and is essential for the development of Myxococcus xanthus. J Bacteriol 1993; 175:4545–4549.

    Google Scholar 

  63. Gill RE, Karlok M, Benton D. Myxococcus xanthus encodes an ATP- dependent protease which is required for developmental gene transcription and intercellular signaling. J Bacteriol 1993; 175:4538–4544.

    Google Scholar 

  64. Riethdorf S, Voider U, Gerth U et al. Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon gene. J Bacteriol 1994; 176:6518–6527.

    Google Scholar 

  65. Schmidt R, Decatur AL, Rather PN et al. Bacillus subtilis Lon protease prevents inappropriate transcription of genes under the control of the sporulation transcription factor σG. J Bacteriol 1994; 176:6528–6537.

    Google Scholar 

  66. Alley MRK, Maddock JR, Shapiro L. Requirement for the carboxyl terminus of a bacterial chemoreceptor for its targeted proteolysis. Science 1993; 239:1754–1757.

    Google Scholar 

  67. Wang N, Gottesman S,.Willingham MC et al. A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc Natl Acad Sci USA 1993; 90:11247–11251.

    Google Scholar 

  68. Suzuki CK, Suda K, Wang N et al. Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration. Science 1994; 264:273–276.

    Google Scholar 

  69. Van Dyck L, Pearce DA, Sherman F. PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae. J Biol Chem 1994; 269:238–242.

    Google Scholar 

  70. Maurizi MR, Trisler P, Gottesman S. Insertional mutagenesis of the lon gene in Escherichia coli: lon is dispensable. J Bacteriol 1985; 164:1124–1135.

    Google Scholar 

  71. Kirby JE, Trempy JE, Gottesman S. Excision of a P4-like cryptic prophage leads to Alp protease expression in Escherichia coli. J Bacteriol 1994; 176:2068–2081.

    Google Scholar 

  72. Trempy JE, Kirby JE, Gottesman S. Alp suppression of Lon: Dependence on the slpA gene. J Bacteriol 1994; 176:2061 – 2067.

    Google Scholar 

  73. Trempy JE, Gottesman S. Alp, a suppressor of lon protease mutants in Escherichia coli. J Bacteriol 1989; 171:3348–3353.

    Google Scholar 

  74. Hwang BJ, Woo KM, Goldberg AL et al. Protease Ti, a new ATP- dependent protease in Escherichia coli contains protein- activated ATPase and proteolytic functions in distinct subunits. J Biol Chem 1988; 263:8727–8734.

    Google Scholar 

  75. Katayama Y, Gottesman S, Pumphrey J et al. The two-component ATP-dependent Clp protease of Escherichia coli: purification, cloning, and mutational analysis of the ATP-binding component. J Biol Chem 1988; 263:15226–15236.

    Google Scholar 

  76. Katayama-Fujimura Y, Gottesman S, Maurizi MR. a multiple component ATP-dependent protease from Escherichia coli. J Biol Chem 1987; 262:4477–4485.

    Google Scholar 

  77. Woo KM, Chung WJ, Ha DB et al. Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides. J Biol Chem 1989; 264:2088 – 2091.

    Google Scholar 

  78. Maurizi MR, Clark WP, Kim S-H et al. ClpP represents a unique family of serine proteases. J Biol Chem 1990; 265:12546 – 12552.

    Google Scholar 

  79. Maurizi MR, Clark WP, Katayama Y et al. Sequence and structure of ClpP, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J Biol Chem 1990; 265:12536 – 12445.

    Google Scholar 

  80. Gottesman S, Clark WP, Maurizi MR. The ATP-dependent Clp protease of Escherichia coli: sequence of clpA and identification of a Op-specific substrate. J Biol Chem 1990; 265:7886–7893.

    Google Scholar 

  81. Gottesman S, Squires C, Pichersky E et al. Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eu-karyotes. Proc Natl Acad Sci USA 1990; 87:3513–3517.

    Google Scholar 

  82. Kroh HE, Simon LE. The ClpP component of Clp protease is the σ32-dependent heat shock protein F21.5. J Bacteriol 1990; 172:6026–6034.

    Google Scholar 

  83. Tobias JW, Shrader TE, Rocap G et al. The N-End rule in bacteria. Science 1991; 254:1374–1376.

    Google Scholar 

  84. Wojtkowiak D, Georgopoulos C, Zylicz M. ClpX, a new specificity component of the ATP-dependent Escherichia coli Clp protease, is potentially involved in λ DNA replication. J Biol Chem 1993; 268:22609–22617.

    Google Scholar 

  85. Gottesman S, Clark WP, de Crecy-Lagard V et al. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. J Biol Chem 1993; 268:22618–22626.

    Google Scholar 

  86. Geuskens V, Mhammedi-Alaoui A, Desmet L et al. Virulence in bacteriophage Mu: a case of trans-dominant proteolysis by the Escherichia coli Clp serine protease. EMBO J 1992; 11:5121 – 5127.

    Google Scholar 

  87. Lehnherr H, Yarmolinsky MB. Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli. Proc Natl Acad Sci USA 1995; 92:3274–3277.

    Google Scholar 

  88. Wickner S, Gottesman S, Skowyra D et al. A molecular chaperone, ClpA, functions like DnaK and DnaJ. Proc Natl Acad Sci USA 1994; 91:12218–12222.

    Google Scholar 

  89. Mhammedi-Alaoui A, Pato M, Gamma M-J et al. A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX protein. Molec Microbiol 1994; 11:1109–1116.

    Google Scholar 

  90. Leuchenko I, Luo L, Baker TA. Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes and Dev 1995; 9:2399–2408.

    Google Scholar 

  91. Damerau K, St. John AC. Role of Clp protease subunits in degradation of carbon starvation proteins in Escherichia coli. J Bacteriol 1993; 175:53–63.

    Google Scholar 

  92. Kitagawa M, Wada C, Yoshioka S et al. Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock a facter (σ32). J Bacteriol 1991; 173:4247–4253.

    Google Scholar 

  93. Squires CL, Pedersen S, Ross BM et al. ClpB is the Escherichia coli heat shock protein F84.1. J Bacteriol 1991; 173:4254–4262.

    Google Scholar 

  94. Sanchez Y, Taulien J, Borkovich KA et al. Hsp104 is required for tolerance to many forms of stress. EMBO J 1992; 11:2357 – 2364.

    Google Scholar 

  95. Parsell DA, Sanchez Y, Stitzel JD et al. Hsp104 is a highly conserved protein with two essential nucleotide-binding sites. Nature 1991; 353:270–273.

    Google Scholar 

  96. Parsell DA, Kowal AS, Singer MA et al. Protein disaggregation mediated by heat-shock protein Hspl04. Nature 1994; 372:475–478.

    Google Scholar 

  97. Kaiser AD. Mutations in a temperate bacteriophage affecting its ability to lysogenize. Escherichia coli. Virology 1957; 3:42-.

    Google Scholar 

  98. Wulff DL, Rosenberg M. Establishment of repressor synthesis. In: Hendrix RW, Roberts JW, Stahl FW, Weisberg RA, eds. Lambda IL Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1983:53–73

    Google Scholar 

  99. Hoyt MA, Knight DM, Das A et al. Control of phage lambda development by stability and synthesis of cII protein: Role of the viral cIII and host hflA, himA and himD genes. Cell 1982; 31:565–573.

    Google Scholar 

  100. Banuett F, Herskowitz I. Identification of polypeptides encoded by an Escherichia coli locus (hflA) that governs the lysis-lysogeny decision of bacteriophage λ. J Bacteriol 1987; 169:4076–4085.

    Google Scholar 

  101. Noble JA, Innis MA, Koonin EV et al. The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain. Proc Natl Acad Sci USA 1993; 90:10866–10870.

    Google Scholar 

  102. Cheng HH, Muhlrad PJ, Hoyt A et al. Cleavage of the cII protein between lysis and lysogeny. Proc Natl Acad Sci USA 1988; 85:7882–7886.

    Google Scholar 

  103. Tomoyasu T, Yuki T, Morimura S et al. The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression. J Bacteriol 1993; 175:1344–1351.

    Google Scholar 

  104. Herman C, Ogura T, Tomoyasu T et al. Cell growth and λ phage development controlled by the same essential Escherichia coli gene, fisH/hflB. Proc Natl Acad Sci USA 1993; 90:10861 – 10865.

    Google Scholar 

  105. Herman C, Thévenet D, D’Ari R et al. Degradation of σ32, the heat shock regulator in Escherichia coli, is governed by HflB. Proc Natl Acad Sci USA 1995; 92:3516–3520.

    Google Scholar 

  106. Tomoyasu T, Gamer J, Bukau B et al. Escherichia coli FtsH is a membrane-bound ATP-dependent protease which degrades the heat-shock transcription factor σ32. EMBO J 1995; 14:2551–2560.

    Google Scholar 

  107. Straus DB, Walter WA, Gross CA. The heat shock response of E. coli is regulated by changes in the concentration of σ32. Nature 1987; 329:348–391.

    Google Scholar 

  108. Bukau B. Regulation of the Escherichia coli heat-shock response. Molec Microbiol 1993; 9:671–680.

    Google Scholar 

  109. Georgopoulos C, Ang D, Liberek K et al. Properties of the Escherichia coli heat shock proteins and their role in bacteriophage λ growth. In: Morimoto RI, Tissieres A, Georgopoulos C, eds. Stress Proteins in Biology and Medicine. New York: Cold Spring Harbor Laboratory Press, 1990:191–221

    Google Scholar 

  110. Craig EA, Gross CA. Is hsp70 the cellular thermometer? Trends Biochem Sci 1991; 16:135–140.

    Google Scholar 

  111. St. John AC, Goldberg AL. Effects of reduced energy production on protein degradation, guanosine tetraphosphate, and RNA synthesis in Escherichia coli. J Biol Chem 1978; 253:2705 – 2711.

    Google Scholar 

  112. Schoulaker-Schwarz R, Dekel-Gorodetsky L, Engelberg-Kulka H. An additional function for bacteriophage λ rex: The rexB product prevents degradation of the λ O protein. Proc Natl Acad Sci USA 1991; 88:4996–5000.

    Google Scholar 

  113. Simon LD, Tomczak K, John ACS. Bacteriophages inhibit degradation of abnormal proteins in E. coli. Nature 1978; 275:424–428.

    Google Scholar 

  114. Sarabhai AS, Stretton AOW, Brenner S et al. Colinearity of the gene with the polypeptide chain. Nature 1964; 201:13–17.

    Google Scholar 

  115. Skorupski K, Tomaschewski J, Ruger W et al. A bacteriophage T4 gene which functions to inhibit Lon protease. J Bacteriol 1988; 170:3016–3024.

    Google Scholar 

  116. Lange R, Hengge-Aronis R. The cellular concentration of the σs subunit of RNA polymerase in Escherichia coli is controlled at the levels of transcription, translation and protein stability. Genes & Develop 1994; 1994:1600–1612.

    Google Scholar 

  117. Lee K-H, Schweder T, Lomovskaya O et al. ClpPX proteolytic activity plays a major role in lowering σ38 levels in exponential phase Escherichia coli. ASM General Meeting Abstracts 1995:509; H-100.

    Google Scholar 

  118. Yura T, Nagai H, Mori H. Regulation of the heat-shock response in bacteria. Annu Rev Microbiol 1993; 47:321–350.

    Google Scholar 

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Gottesman, S. (1996). Roles for Energy-Dependent Proteases in Regulatory Cascades. In: Regulation of Gene Expression in Escherichia coli . Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8601-8_24

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  • DOI: https://doi.org/10.1007/978-1-4684-8601-8_24

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