메뉴 건너뛰기




Volumn 181, Issue 7, 1999, Pages 2236-2243

A conserved domain in Escherichia coli Lon protease is involved in substrate discriminator activity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIOPHAGE; CELL DIVISION; DNA DAMAGE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; GENETIC TRANSCRIPTION; MUTAGENESIS; OPEN READING FRAME; PHENOTYPE; PLASMID; POINT MUTATION; PRIORITY JOURNAL; PROBABILITY; PROTEIN CONFORMATION;

EID: 0032910867     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.7.2236-2243.1999     Document Type: Article
Times cited : (55)

References (65)
  • 1
    • 0025455942 scopus 로고
    • Cloning, structure and expression of the full-size lon gene in Escherichia coli coding for ATP-dependent La-proteinase
    • Amerik, A., V. K. Antonov, N. I. Ostroumova, T. V. Rotanova, and L. G. Chistiakova. 1990. Cloning, structure and expression of the full-size lon gene in Escherichia coli coding for ATP-dependent La-proteinase. Bioorg. Khim. 16:869-880.
    • (1990) Bioorg. Khim. , vol.16 , pp. 869-880
    • Amerik, A.1    Antonov, V.K.2    Ostroumova, N.I.3    Rotanova, T.V.4    Chistiakova, L.G.5
  • 3
    • 0016719491 scopus 로고
    • Mutation blocking the specific degradation of reinitiation polypeptides in E. coli
    • Apte, B. N., H. Rhodes, and D. Zipser. 1975. Mutation blocking the specific degradation of reinitiation polypeptides in E. coli. Nature 257:329-331.
    • (1975) Nature , vol.257 , pp. 329-331
    • Apte, B.N.1    Rhodes, H.2    Zipser, D.3
  • 4
    • 0023933251 scopus 로고
    • Fine-structure mapping and identification of two regulators of capsule synthesis in Escherichia coli K-12
    • Brill, J. A., C. Quinlan-Walshe, and S. Gottesman. 1988. Fine-structure mapping and identification of two regulators of capsule synthesis in Escherichia coli K-12. J. Bacteriol. 170:2599-2611.
    • (1988) J. Bacteriol. , vol.170 , pp. 2599-2611
    • Brill, J.A.1    Quinlan-Walshe, C.2    Gottesman, S.3
  • 5
    • 0015810658 scopus 로고
    • Mutants of Escherichia coli with a defect in the degradation of nonsense fragments
    • Bukhari, A. I., and D. Zipser. 1973. Mutants of Escherichia coli with a defect in the degradation of nonsense fragments. Nature 243:238-241.
    • (1973) Nature , vol.243 , pp. 238-241
    • Bukhari, A.I.1    Zipser, D.2
  • 7
    • 0019859345 scopus 로고
    • ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12
    • Charette, M. F., G. W. Henderson, and A. Markovitz. 1981. ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 78:4728-4732.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4728-4732
    • Charette, M.F.1    Henderson, G.W.2    Markovitz, A.3
  • 8
    • 0023790425 scopus 로고
    • Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La
    • Chin, D. T., S. A. Goff, T. Webster, T. Smith, and A. L. Goldberg. 1988. Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La. J. Biol. Chem. 263:11718-11728.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11718-11728
    • Chin, D.T.1    Goff, S.A.2    Webster, T.3    Smith, T.4    Goldberg, A.L.5
  • 9
    • 0013533949 scopus 로고
    • The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La
    • Chung, C. H., and A. L. Goldberg. 1981. The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Proc. Natl. Acad. Sci. USA 78:4931-4935.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4931-4935
    • Chung, C.H.1    Goldberg, A.L.2
  • 10
    • 0020093926 scopus 로고
    • DNA stimulates ATP-dependent proteolysis and protein-dependent ATPase activity of protease La from Escherichia coli
    • Chung, C. H., and A. L. Goldberg. 1982. DNA stimulates ATP-dependent proteolysis and protein-dependent ATPase activity of protease La from Escherichia coli. Proc. Natl. Acad. Sci. USA 79:795-799.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 795-799
    • Chung, C.H.1    Goldberg, A.L.2
  • 11
    • 0025646664 scopus 로고
    • Saturation and specificity of the Lon protease of Escherichia coli
    • Dervyn, E., D. Canceill, and O. Huisman. 1990. Saturation and specificity of the Lon protease of Escherichia coli. J. Bacteriol. 172:7098-7103.
    • (1990) J. Bacteriol. , vol.172 , pp. 7098-7103
    • Dervyn, E.1    Canceill, D.2    Huisman, O.3
  • 12
    • 0029767414 scopus 로고    scopus 로고
    • Identification of a second RcsA protein, a positive regulator of colanic acid capsular polysaccharide genes, in Escherichia coli
    • Dierksen, K. P., and J. E. Trempy. 1996. Identification of a second RcsA protein, a positive regulator of colanic acid capsular polysaccharide genes, in Escherichia coli. J. Bacteriol. 178:5053-5056.
    • (1996) J. Bacteriol. , vol.178 , pp. 5053-5056
    • Dierksen, K.P.1    Trempy, J.E.2
  • 13
    • 0032925895 scopus 로고    scopus 로고
    • Escherichia coli RcsA, a positive activator of colanic acid capsular polysaccharide synthesis, functions to activate its own expression
    • Ebel, W., and J. E. Trempy. 1999. Escherichia coli RcsA, a positive activator of colanic acid capsular polysaccharide synthesis, functions to activate its own expression. J. Bacteriol. 181:577-584.
    • (1999) J. Bacteriol. , vol.181 , pp. 577-584
    • Ebel, W.1    Trempy, J.E.2
  • 14
    • 0028061755 scopus 로고
    • A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli
    • Fischer, H., and R. Glockshuber. 1994. A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli. FEBS Lett. 356:101-103.
    • (1994) FEBS Lett. , vol.356 , pp. 101-103
    • Fischer, H.1    Glockshuber, R.2
  • 15
    • 0031015304 scopus 로고    scopus 로고
    • Bacterial protease Lon is a site-specific DNA-binding protein
    • Fu, G. K., M. J. Smith, and D. M. Markovitz. 1997. Bacterial protease Lon is a site-specific DNA-binding protein. J. Biol. Chem. 272:534-538.
    • (1997) J. Biol. Chem. , vol.272 , pp. 534-538
    • Fu, G.K.1    Smith, M.J.2    Markovitz, D.M.3
  • 17
    • 0016816177 scopus 로고
    • Prophage induction and cell division in E. coli. III. Mutations in sfiA and sfiB restore division in tif and lon strains and permit the mutator properties of tif
    • George, J., M. Castellazzi, and G. Buttin. 1975. Prophage induction and cell division in E. coli. III. Mutations in sfiA and sfiB restore division in tif and lon strains and permit the mutator properties of tif. Mol. Gen. Genet. 140:309-332.
    • (1975) Mol. Gen. Genet. , vol.140 , pp. 309-332
    • George, J.1    Castellazzi, M.2    Buttin, G.3
  • 18
    • 0023216021 scopus 로고
    • An increased content of protease La, the lon gene product, increases protein degradation and blocks growth in Escherichia coli
    • Goff, S. A., and A. L. Goldberg. 1987. An increased content of protease La, the lon gene product, increases protein degradation and blocks growth in Escherichia coli. J. Biol. Chem. 262:4508-4515.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4508-4515
    • Goff, S.A.1    Goldberg, A.L.2
  • 19
    • 0026503828 scopus 로고
    • The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
    • Goldberg, A. L. 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
  • 21
    • 0022360054 scopus 로고
    • The role of ATP hydrolysis in the breakdown of proteins and peptides by protease La from Escherichia coli
    • Goldberg, A. L., and L. Waxman. 1985. The role of ATP hydrolysis in the breakdown of proteins and peptides by protease La from Escherichia coli. J. Biol. Chem. 260:12029-12034.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12029-12034
    • Goldberg, A.L.1    Waxman, L.2
  • 22
    • 0024811752 scopus 로고
    • Genetics of proteolysis in Escherichia coli
    • Gottesman, S. 1989. Genetics of proteolysis in Escherichia coli. Annu. Rev. Genet. 23:163-198.
    • (1989) Annu. Rev. Genet. , vol.23 , pp. 163-198
    • Gottesman, S.1
  • 23
    • 0000871346 scopus 로고
    • Regulation of capsule synthesis: Modification of the two-component paradigm by an accessory unstable regulator
    • J. A. Hoch and T. J. Silhavy (ed.). Washington, D.C.
    • Gottesman, S. 1995. Regulation of capsule synthesis: modification of the two-component paradigm by an accessory unstable regulator, p. 253-262. In J. A. Hoch and T. J. Silhavy (ed.). Two-component signal transduction. American Society for Microbiology, Washington, D.C.
    • (1995) Two-component Signal Transduction. American Society for Microbiology , pp. 253-262
    • Gottesman, S.1
  • 24
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman, S. 1996. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:465-506.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 25
    • 0019842601 scopus 로고
    • Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12
    • Gottesman, S., E. Halpern, and P. Trisler. 1981. Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12. J. Bacteriol. 148:265-273.
    • (1981) J. Bacteriol. , vol.148 , pp. 265-273
    • Gottesman, S.1    Halpern, E.2    Trisler, P.3
  • 26
    • 0026454716 scopus 로고
    • Regulation by proteolysis: Energy-dependent proteases and their targets
    • Gottesman, S., and M. R. Maurizi. 1992. Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol. Rev. 56:592-621.
    • (1992) Microbiol. Rev. , vol.56 , pp. 592-621
    • Gottesman, S.1    Maurizi, M.R.2
  • 27
    • 0025866063 scopus 로고
    • Regulation of capsular polysaccharide synthesis in Escherichia coli K12
    • Gottesman, S., and V. Stout. 1991. Regulation of capsular polysaccharide synthesis in Escherichia coli K12. Mol. Microbiol. 5:1599-1606.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1599-1606
    • Gottesman, S.1    Stout, V.2
  • 28
    • 0021878094 scopus 로고
    • Regulation of capsular polysaccharide synthesis in Escherichia coli K-12: Characterization of three regulatory genes
    • Gottesman, S., P. Trisler, and A. Torres-Cabassa. 1985. Regulation of capsular polysaccharide synthesis in Escherichia coli K-12: characterization of three regulatory genes. J. Bacteriol. 162:1111-1119.
    • (1985) J. Bacteriol. , vol.162 , pp. 1111-1119
    • Gottesman, S.1    Trisler, P.2    Torres-Cabassa, A.3
  • 29
    • 0021878094 scopus 로고
    • Regulation of capsular polysaccharide synthesis in Escherichia coli K-12: Characterization of three regulatory genes
    • Gottesman, S., P. Trisler, and A. Torres-Cabassa. 1985. Regulation of capsular polysaccharide synthesis in Escherichia coli K-12: characterization of three regulatory genes. J. Bacteriol. 162:1111-1119.
    • (1985) J. Bacteriol. , vol.162 , pp. 1111-1119
    • Gottesman, S.1    Trisler, P.2    Torres-Cabassa, A.3
  • 30
    • 0017863123 scopus 로고
    • Deg phenotype of Escherichia coli lon mutants
    • Gottesman, S., and D. Zipser. 1978. Deg phenotype of Escherichia coli lon mutants. J. Bacteriol. 133:844-851.
    • (1978) J. Bacteriol. , vol.133 , pp. 844-851
    • Gottesman, S.1    Zipser, D.2
  • 31
    • 0020647421 scopus 로고
    • Mutations in the lon gene of E. coli K-12 phenotypically suppress a mutation in the sigma subunit of RNA polymerase
    • Grossman, A. D., R. R. Burgess, W. Walter, and C. A. Gross. 1983. Mutations in the lon gene of E. coli K-12 phenotypically suppress a mutation in the sigma subunit of RNA polymerase. Cell 32:151-159.
    • (1983) Cell , vol.32 , pp. 151-159
    • Grossman, A.D.1    Burgess, R.R.2    Walter, W.3    Gross, C.A.4
  • 32
    • 0031982642 scopus 로고    scopus 로고
    • Isolation and characterization of the phage T4 PinA protein, an inhibitor of the ATP-dependent Lon protease of Escherichia coli
    • Hilliard, J. J., M. R. Maurizi, and L. D. Simon. 1998. Isolation and characterization of the phage T4 PinA protein, an inhibitor of the ATP-dependent Lon protease of Escherichia coli. J. Biol. Chem 273:518-523.
    • (1998) J. Biol. Chem , vol.273 , pp. 518-523
    • Hilliard, J.J.1    Maurizi, M.R.2    Simon, L.D.3
  • 33
    • 0031982708 scopus 로고    scopus 로고
    • PinA inhibits ATP hydrolysis and energy-dependent protein degradation by Lon protease
    • Hilliard, J. J., L. D. Simon, L. Van Melderen, and M. R. Maurizi. 1998. PinA inhibits ATP hydrolysis and energy-dependent protein degradation by Lon protease. J. Biol. Chem. 273:524-527.
    • (1998) J. Biol. Chem. , vol.273 , pp. 524-527
    • Hilliard, J.J.1    Simon, L.D.2    Van Melderen, L.3    Maurizi, M.R.4
  • 34
    • 0001107759 scopus 로고
    • A locus that controls filament formation and sensitivity to radiation in Escherichia coli K12
    • Howard-Flanders, P., E. Simson, and L. Theriot. 1964. A locus that controls filament formation and sensitivity to radiation in Escherichia coli K12. Genetics 49:237-246.
    • (1964) Genetics , vol.49 , pp. 237-246
    • Howard-Flanders, P.1    Simson, E.2    Theriot, L.3
  • 35
    • 0019119526 scopus 로고
    • Further characterization of sfiA and sfiB mutation in Escherichia coli
    • Huisman, O., R. D'Ari, and J. George. 1980. Further characterization of sfiA and sfiB mutation in Escherichia coli. J. Bacteriol. 144:185-191.
    • (1980) J. Bacteriol. , vol.144 , pp. 185-191
    • Huisman, O.1    D'Ari, R.2    George, J.3
  • 36
    • 0344321693 scopus 로고
    • Cell-division control in Escherichia coli: Specific induction of the SOS function SfiA protein is sufficient to block septation
    • Huisman, O., R. D'Ari, and S. Gottesman. 1984. Cell-division control in Escherichia coli: specific induction of the SOS function SfiA protein is sufficient to block septation. Proc. Natl. Acad. Sci. USA 81:4490-4494.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4490-4494
    • Huisman, O.1    D'Ari, R.2    Gottesman, S.3
  • 37
    • 0019829757 scopus 로고
    • An inducible DNA-replication-cell division coupling mechanism in E. coli
    • Huisman, O., and R. D'Ari. 1981. An inducible DNA-replication-cell division coupling mechanism in E. coli. Nature 290:797-799.
    • (1981) Nature , vol.290 , pp. 797-799
    • Huisman, O.1    D'Ari, R.2
  • 38
    • 0022408210 scopus 로고
    • Role of the SulB (FtsZ) protein in division inhibition during the SOS response in Escherichia coli: FtsZ stabilizes the inhibitor SulA in maxicells
    • Jones, C., and I. B. Holland. 1985. 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 82:6045-6049.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6045-6049
    • Jones, C.1    Holland, I.B.2
  • 39
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • Lupas, A. 1996. Prediction and analysis of coiled-coil structures. Methods Enzymol. 266:513-525.
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 40
    • 0026356891 scopus 로고
    • Predicting coiled-coils from protein sequences
    • Lupas, A., M. V. 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    Dyke, M.V.2    Stock, J.3
  • 41
    • 0022627940 scopus 로고
    • Overproduction of FtsZ suppresses sensitivity of lon mutants to division inhibition
    • Lutkenhaus, J., B. Sanjanwala, and M. Lowe. 1986. Overproduction of FtsZ suppresses sensitivity of lon mutants to division inhibition. J. Bacteriol. 166:756-762.
    • (1986) J. Bacteriol. , vol.166 , pp. 756-762
    • Lutkenhaus, J.1    Sanjanwala, B.2    Lowe, M.3
  • 42
    • 0344073475 scopus 로고
    • Regulatory mechanisms for the synthesis of capsular polysaccharide in mucoid mutants of Escherichia coli K-12
    • Markovitz, A. 1964. Regulatory mechanisms for the synthesis of capsular polysaccharide in mucoid mutants of Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 51:239-246.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 239-246
    • Markovitz, A.1
  • 43
    • 0026601663 scopus 로고
    • Proteases and protein degradation in Escherichia coli
    • Maurizi, M. R. 1992. Proteases and protein degradation in Escherichia coli. Experientia 48:178-201.
    • (1992) Experientia , vol.48 , pp. 178-201
    • Maurizi, M.R.1
  • 44
    • 0022405836 scopus 로고
    • Insertional mutagenesis of the lon gene in Escherichia coli: Lon is dispensable
    • Maurizi, M. R., P. Trisler, and S. Gottesman. 1985. Insertional mutagenesis of the lon gene in Escherichia coli: lon is dispensable. J. Bacteriol. 164:1124-1135.
    • (1985) J. Bacteriol. , vol.164 , pp. 1124-1135
    • Maurizi, M.R.1    Trisler, P.2    Gottesman, S.3
  • 45
  • 46
    • 0020651799 scopus 로고
    • Protein degradation in Escherichia coli: The lon gene controls the stability of SulA protein
    • Mizusawa, S., and S. Gottesman. 1983. Protein degradation in Escherichia coli: the lon gene controls the stability of SulA protein. Proc. Natl. Acad. Sci. USA 80:358-362.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 358-362
    • Mizusawa, S.1    Gottesman, S.2
  • 47
    • 0027765577 scopus 로고
    • An imbalance of HU synthesis induces mucoidy in Escherichia coli
    • Painbeni, E., E. Mouray, S. Gottesman, and J. Rouviere-Yaniv. 1993. An imbalance of HU synthesis induces mucoidy in Escherichia coli. J. Mol. Biol. 234:1021-1037.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1021-1037
    • Painbeni, E.1    Mouray, E.2    Gottesman, S.3    Rouviere-Yaniv, J.4
  • 48
    • 0020446736 scopus 로고
    • Coiled-coils in alpha-helix-containing proteins: Analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins
    • Parry, D. A. D. 1982. Coiled-coils in alpha-helix-containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins. Biosci. Rep. 2:1017-1024.
    • (1982) Biosci. Rep. , vol.2 , pp. 1017-1024
    • Parry, D.A.D.1
  • 50
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 53
    • 0023942606 scopus 로고
    • A bacteriophage T4 gene which functions to inhibit Escherichia coli Lon protease
    • Skorupski, K., J. Tomaschewski, W. Ruger, and L. D. Simon. 1988. A bacteriophage T4 gene which functions to inhibit Escherichia coli Lon protease. J. Bacteriol. 170:3016-3024.
    • (1988) J. Bacteriol. , vol.170 , pp. 3016-3024
    • Skorupski, K.1    Tomaschewski, J.2    Ruger, W.3    Simon, L.D.4
  • 54
    • 0028957883 scopus 로고
    • A small RNA acts as an antisilencer of the H-NS-silenced rcsA gene of Escherichia coli
    • Sledjeski, D., and S. Gottesman. 1995. A small RNA acts as an antisilencer of the H-NS-silenced rcsA gene of Escherichia coli. Proc. Natl. Acad. Sci. USA 92:2003-2007.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2003-2007
    • Sledjeski, D.1    Gottesman, S.2
  • 55
    • 0032579436 scopus 로고    scopus 로고
    • Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme
    • Starkova, N. N., E. P. Koroleva, L. D. Runsh, L. M. Ginodman, and T. V. Rotanova. 1998. Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme. FEBS Lett. 422: 218-220.
    • (1998) FEBS Lett. , vol.422 , pp. 218-220
    • Starkova, N.N.1    Koroleva, E.P.2    Runsh, L.D.3    Ginodman, L.M.4    Rotanova, T.V.5
  • 56
  • 57
    • 0022383165 scopus 로고
    • A method for the efficient blotting of strongly basic proteins from sodium dodecyl sulfate-polyacrylamide gels to nitrocellulose
    • Szewczyk, B., and L. M. Kozloff. 1985. A method for the efficient blotting of strongly basic proteins from sodium dodecyl sulfate-polyacrylamide gels to nitrocellulose. Anal. Biochem. 150:403-407.
    • (1985) Anal. Biochem. , vol.150 , pp. 403-407
    • Szewczyk, B.1    Kozloff, L.M.2
  • 58
    • 0023131531 scopus 로고
    • Capsule synthesis in Escherichia coli K-12 is regulated by proteolysis
    • Torres-Cabassa, A. S., and S. Gottesman. 1987. Capsule synthesis in Escherichia coli K-12 is regulated by proteolysis. J. Bacteriol. 169:981-989.
    • (1987) J. Bacteriol. , vol.169 , pp. 981-989
    • Torres-Cabassa, A.S.1    Gottesman, S.2
  • 59
    • 0024319460 scopus 로고
    • Alp, a suppressor of lon protease mutants in Escherichia coli
    • Trempy, J. E., and S. Gottesman. 1989. Alp, a suppressor of lon protease mutants in Escherichia coli. J. Bacteriol. 171:3348-3353.
    • (1989) J. Bacteriol. , vol.171 , pp. 3348-3353
    • Trempy, J.E.1    Gottesman, S.2
  • 60
    • 0021184998 scopus 로고
    • Lon transcriptional regulation of genes necessary for capsular polysaccharide synthesis in Escherichia coli K-12
    • Trisler, P., and S. Gottesman. 1984. lon transcriptional regulation of genes necessary for capsular polysaccharide synthesis in Escherichia coli K-12. J. Bacteriol 160:184-191.
    • (1984) J. Bacteriol , vol.160 , pp. 184-191
    • Trisler, P.1    Gottesman, S.2
  • 61
    • 0001939048 scopus 로고
    • The SOS response of Escherichia coli
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaecter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Walker, G. C. 1987. The SOS response of Escherichia coli, p. 1346-1357. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaecter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular Biology. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1346-1357
    • Walker, G.C.1
  • 62
    • 0020294051 scopus 로고
    • Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion
    • Waxman, L., and A. L. Goldberg. 1982. Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion. Proc. Natl. Acad. Sci. USA 79:4883-4887.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4883-4887
    • Waxman, L.1    Goldberg, A.L.2
  • 63
    • 0022413419 scopus 로고
    • Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction
    • Waxman, L., and A. L. Goldberg. 1985. Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction. J. Biol. Chem. 260:12022-12028.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12022-12028
    • Waxman, L.1    Goldberg, A.L.2
  • 64
    • 0022520796 scopus 로고
    • Selectivity of intracellular proteolysis: Protein substrates activate the ATP-dependent protease (La)
    • Waxman, L., and A. L. Goldberg. 1986. Selectivity of intracellular proteolysis: protein substrates activate the ATP-dependent protease (La). Science 232:500-503.
    • (1986) Science , vol.232 , pp. 500-503
    • Waxman, L.1    Goldberg, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.