Lactose metabolism

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General

  • Pure Clones of Lactose-negative mutants obtained in Escherichia coli after treatment with 5-bromouracil[1]
  • Recombination analysis of bacterial heredity[2]
  • Allelic Relationships and Reverse Mutation in Escherichia Coli[3]
  • Transposition of the lac region of Escherichia coli. I. Inversion of the lac operon and transduction of lac by phi80[4]
  • Transposition of the Lac region of E. coli[5]
  • Mutational alteration of the maximal level of Lac operon expression[6]
  • Frameshift mutations in the lactose operon of E. coli[7]
  • Mutagens which cause deletions in Escherichia coli[8]

Papers about the Promoter, Operator, and General Regulation of Lactose Metabolism

  • Genetic regulatory mechanisms in the synthesis of proteins[9]
  • A DELETION ANALYSIS OF THE LAC OPERATOR REGION IN ESCHERICHIA COLI[10]
  • Comparison of beta-galactosidases from normal (i-o+z+) and operator constitutive (i-ocz+) strains of E. coli[11]
  • Allelic amber and ochre suppressors[12]
  • RESTORATION OF OPERON ACTIVITY BY SUPPRESSORS[13]
  • Genetic mapping of the regulator and operator genes of the lac operon[14]
  • Genetic evidence that the operator locus is distinct from the the z gene in the lac operon of Escherichia coli[15]
  • New controlling element in the Lac operon of E. coli[16]
  • The promoter-operator region of the lac operon of Escherichia coli[17]
  • Biochemical evidence that the operator locus is distinct from the z gene in the lac operon of Escherichia coli[18]
  • The Nature of Mutants in the lac Promoter Region[19]

Papers about the Polarity of the lac Operon

  • A polycistronic messenger RNA associated with beta-galactosidase induction[20]
  • Nonsense mutants and polarity in the lac operon of Escherichia coli[21]
  • Transduction by bacteriophage P-1 and the properties of the lac genetic region in E. coli and S. dysenteriae[22]
  • The influence of deletions on polarity[23]

lacI

  • On the nature of the repressor of beta-galactosidase synthesis in Escherichia coli[24]
  • NON-INDUCIBLE MUTANTS OF THE REGULATOR GENE IN THE "LACTOSE" SYSTEM OF ESCHERICHIA COLI[25]
  • The genetic control and cytoplasmic expression of “Inducibility” in the synthesis of β-galactosidase by E. coli[26]
  • Direction of transcription of a regulatory gene in E. coli[27]
  • Suppressible regulator constitutive mutants of the lactose system in Escherichia coli[28]
  • Isolation of the lac repressor[29]
  • Mutants that make more lac repressor[30]
  • Suppression of and complementation among mutants of the regulatory gene of the lactose operon of Escherichia coli[31]
  • DNA sequence for a low-level promoter of the lac repressor gene and an 'up' promoter mutation[32]
  • Genetic studies of the lac repressor. VIII. DNA sequence change resulting from an intragenic duplication[33]
  • Lac repressor and lac operator[34]
  • Lac repressor[35]
  • How lac repressor binds to DNA[36]
  • The lac repressor-operator interaction. VII. A repressor with unique binding properties: the X86 repressor[37]
  • Lac repressor-operator interaction. V. Characterization of super- and pseudo-wild-type repressors[38]
  • lac Repressor-operator interaction. VI. The natural inducer of the lac operon[39]
  • Mutations affecting the quaternary structure of the lac repressor[40]
  • Genetic map of the lactose repressor gene (i) of Escherichia coli[41]
  • Altered sequences changing the operator-binding properties of the Lac repressor: colinearity of the repressor protein with the i-gene map[42]
  • Translational reinitiation: reinitiation of lac repressor fragments at three internal sites early in the lac i gene of Escherichia coli[43]

lacZ

  • The beta-galactosidase of lactose mutants of Escherichia coli, K-12[44]
  • MULTIPLE MOLECULAR FORMS OF BETA-GALACTOSIDASE[45]
  • THE ORDER OF INDUCTION AND DEINDUCTION OF THE ENZYMES OF THE LACTOSE OPERON IN E. COLI[46]
  • EVIDENCE FOR NONIDENTICAL CHAINS IN THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12[47]
  • Inhibition of the synthesis of beta-galactosidase in Escherichia coli by 2-nitrophenyl-beta-D-fucoside[48]
  • A mutation which creates a new site for the re-initiation of polypeptide synthesis in the z gene of the lac operon of Escherichia coli[49]
  • Co-linearity of beta-galactosidase with its gene by immunological detection of incomplete polypeptide chains[50]
  • Effects of Dimethylsulfoxide on the Lactose Operon in Escherichia coli[51]
  • Beta-galactosidase: orientation and the carboxyl-terminal coding site in the gene[52]
  • Beta-galactosidase: isolation of and antibodies to incomplete chains[53]
  • Beta-galactosidase. In vivo -complementation[54]
  • Construction and properties of Escherichia coli strains exhibiting -complementation of -galactosidase fragments in vivo[55]
  • Genetic and biochemical characterization of some missense mutations in the lacZ gene of Escherichia coli K-12[56]
  • Genetic and enzymatic experiments relating to the quaternary structure of beta-galactosidase[57]
  • Mutation spectra and the neutrality of mutations[58]
  • Genetic and enzymatic experiments relating to the tertiary structure of beta-galactosidase[59]
  • Genetic evidence for the disposition of the substrate binding site of beta-galactosidase[60]

lacY

  • Isolation, genetic analysis, and characterization of Escherichia coli mutants with defects in the lacY gene[61]
  • Interaction of sugars with the membrane protein component of the lactose transport system of Escherichia coli[62]
  • Defective lactose utilization by a mutant of Escherichia coli energy-uncoupled for lactose transport. The advantages of active transport versus facilitated diffusion.[63]
  • A mutant in Escherichia coli energy-uncoupled for lactose transport defect in the lactose-operon[64]
  • Specific labeling and partial purification of the M protein, a component of the beta-galactoside transport system of Escherichia coli[65]
  • The nature of mutants in the lac promoter region[19]
  • GENETIC CONTROL OF THE MEMBRANE PROTEIN COMPONENT OF THE LACTOSE TRANSPORT SYSTEM OF Escherichia coli[66]
  • Direct measurement of the binding of labeled sugars to the lactose permease M protein[67]
  • Temperature-sensitive mutants of Escherichia coli affecting beta-galactoside transport.[68]

lacA

  • Thiogalactoside transacetylase[69]
  • Transposition of the lac region of Escherichia coli. II. On the role of thiogalactoside transacetylase in lactose metabolism[70]
  • Substrate specificity and kinetic studies on thiogalactoside transacetylase[71]
  • Thiogalactoside transacetylase. Amino- and carboxyl-terminal studies[72]
  • Thiogalactoside transacetylase. Physical and chemical studies of subunit structure[73]
  • Thiogalactoside transacetylase of the lactose operon as an enzyme for detoxification[74]

Procedures

  • A SPECTROPHOTOMETRIC ASSAY FOR THIOGALACTOSIDE TRANSACETYLASE[75]
  • PURIFICATION, COMPOSITION, AND MOLECULAR WEIGHT OF THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12[76]

References

  1. ↑ WITKIN, EM & SICURELLA, NA (1964) PURE CLONES OF LACTOSE-NEGATIVE MUTANTS OBTAINED IN ESCHERICHIA COLI AFTER TREATMENT WITH 5-BROMOURACIL. J. Mol. Biol. 8 610-3 PubMed OMPwiki page
  2. ↑ LEDERBERG, J et al. (1951) Recombination analysis of bacterial heredity. Cold Spring Harb. Symp. Quant. Biol. 16 413-43 PubMed OMPwiki page
  3. ↑ Lederberg, EM (1952) Allelic Relationships and Reverse Mutation in Escherichia Coli. Genetics 37 469-83 PubMed OMPwiki page
  4. ↑ Beckwith, JR & Signer, ER (1966) Transposition of the lac region of Escherichia coli. I. Inversion of the lac operon and transduction of lac by phi80. J. Mol. Biol. 19 254-65 PubMed OMPwiki page
  5. ↑ Beckwith, JR et al. (1966) Transposition of the Lac region of E. coli. Cold Spring Harb. Symp. Quant. Biol. 31 393-401 PubMed OMPwiki page
  6. ↑ Scaife, J & Beckwith, JR (1966) Mutational alteration of the maximal level of Lac operon expression. Cold Spring Harb. Symp. Quant. Biol. 31 403-8 PubMed OMPwiki page
  7. ↑ Malamy, MH (1966) Frameshift mutations in the lactose operon of E. coli. Cold Spring Harb. Symp. Quant. Biol. 31 189-201 PubMed OMPwiki page
  8. ↑ Schwartz, DO & Beckwith, JR (1969) Mutagens which cause deletions in Escherichia coli. Genetics 61 371-6 PubMed OMPwiki page
  9. ↑ JACOB, F & MONOD, J (1961) Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3 318-56 PubMed OMPwiki page
  10. ↑ BECKWITH, JR (1964) A DELETION ANALYSIS OF THE LAC OPERATOR REGION IN ESCHERICHIA COLI. J. Mol. Biol. 8 427-30 PubMed OMPwiki page
  11. ↑ Steers, E Jr et al. (1965) Comparison of beta-galactosidases from normal (i-o+z+) and operator constitutive (i-ocz+) strains of E. coli. Proc. Natl. Acad. Sci. U.S.A. 54 1174-81 PubMed OMPwiki page
  12. ↑ Ohlsson, BM et al. (1968) Allelic amber and ochre suppressors. J. Mol. Biol. 36 209-18 PubMed OMPwiki page
  13. ↑ BECKWITH, J (1963) RESTORATION OF OPERON ACTIVITY BY SUPPRESSORS. Biochim. Biophys. Acta 76 162-4 PubMed OMPwiki page
  14. ↑ Davies, J & Jacob, F (1968) Genetic mapping of the regulator and operator genes of the lac operon. J. Mol. Biol. 36 413-7 PubMed OMPwiki page
  15. ↑ Reznikoff, WS & Beckwith, JR (1969) Genetic evidence that the operator locus is distinct from the the z gene in the lac operon of Escherichia coli. J. Mol. Biol. 43 215-8 PubMed OMPwiki page
  16. ↑ Ippen, K et al. (1968) New controlling element in the Lac operon of E. coli. Nature 217 825-7 PubMed OMPwiki page
  17. ↑ Miller, JH et al. (1968) The promoter-operator region of the lac operon of Escherichia coli. J. Mol. Biol. 38 413-20 PubMed OMPwiki page
  18. ↑ Bhorjee, JS et al. (1969) Biochemical evidence that the operator locus is distinct from the z gene in the lac operon of Escherichia coli. J. Mol. Biol. 43 219-22 PubMed OMPwiki page
  19. ↑ 19.0 19.1 Arditti, RR et al. (1968) The nature of mutants in the lac promoter region. J. Mol. Biol. 38 421-6 PubMed OMPwiki page
  20. ↑ Kiho, Y & Rich, A (1965) A polycistronic messenger RNA associated with beta-galactosidase induction. Proc. Natl. Acad. Sci. U.S.A. 54 1751-8 PubMed OMPwiki page
  21. ↑ Newton, WA et al. (1965) Nonsense mutants and polarity in the lac operon of Escherichia coli. J. Mol. Biol. 14 290-6 PubMed OMPwiki page
  22. ↑ FRANKLIN, NC & LURIA, SE (1961) Transduction by bacteriophage P-1 and the properties of the lac genetic region in E. coli and S. dysenteriae. Virology 15 299-311 PubMed OMPwiki page
  23. ↑ Zipser, D & Newton, A (1967) The influence of deletions on polarity. J. Mol. Biol. 25 567-9 PubMed OMPwiki page
  24. ↑ PARDEE, AB & PRESTIDGE, LS (1959) On the nature of the repressor of beta-galactosidase synthesis in Escherichia coli. Biochim. Biophys. Acta 36 545-7 PubMed OMPwiki page
  25. ↑ WILLSON, C et al. (1964) NON-INDUCIBLE MUTANTS OF THE REGULATOR GENE IN THE "LACTOSE" SYSTEM OF ESCHERICHIA COLI. J. Mol. Biol. 8 582-92 PubMed OMPwiki page
  26. ↑ () PubMed OMPwiki page
  27. ↑ Miller, JH et al. (1968) Direction of transcription of a regulatory gene in E. coli. Nature 220 1287-90 PubMed OMPwiki page
  28. ↑ Müller-Hill, B (1966) Suppressible regulator constitutive mutants of the lactose system in Escherichia coli. J. Mol. Biol. 15 374-6 PubMed OMPwiki page
  29. ↑ Gilbert, W & Müller-Hill, B (1966) Isolation of the lac repressor. Proc. Natl. Acad. Sci. U.S.A. 56 1891-8 PubMed OMPwiki page
  30. ↑ Müller-Hill, B et al. (1968) Mutants that make more lac repressor. Proc. Natl. Acad. Sci. U.S.A. 59 1259-64 PubMed OMPwiki page
  31. ↑ Bourgeois, S et al. (1965) Suppression of and complementation among mutants of the regulatory gene of the lactose operon of Escherichia coli. J. Mol. Biol. 14 300-2 PubMed OMPwiki page
  32. ↑ Calos, MP (1978) DNA sequence for a low-level promoter of the lac repressor gene and an 'up' promoter mutation. Nature 274 762-5 PubMed OMPwiki page
  33. ↑ Calos, MP et al. (1978) Genetic studies of the lac repressor. VIII. DNA sequence change resulting from an intragenic duplication. J. Mol. Biol. 126 865-9 PubMed OMPwiki page
  34. ↑ Müller-Hill, B (1975) Lac repressor and lac operator. Prog. Biophys. Mol. Biol. 30 227-52 PubMed OMPwiki page
  35. ↑ Müller-Hill, B (1971) Lac repressor. Angew. Chem. Int. Ed. Engl. 10 160-72 PubMed OMPwiki page
  36. ↑ Adler, K et al. (1972) How lac repressor binds to DNA. Nature 237 322-7 PubMed OMPwiki page
  37. ↑ Jobe, A & Bourgeois, S (1972) The lac repressor-operator interaction. VII. A repressor with unique binding properties: the X86 repressor. J. Mol. Biol. 72 139-52 PubMed OMPwiki page
  38. ↑ Jobe, A et al. (1972) Lac repressor-operator interaction. V. Characterization of super- and pseudo-wild-type repressors. J. Mol. Biol. 64 181-99 PubMed OMPwiki page
  39. ↑ Jobe, A & Bourgeois, S (1972) lac Repressor-operator interaction. VI. The natural inducer of the lac operon. J. Mol. Biol. 69 397-408 PubMed OMPwiki page
  40. ↑ Schmitz, A et al. (1976) Mutations affecting the quaternary structure of the lac repressor. J. Biol. Chem. 251 3359-66 PubMed OMPwiki page
  41. ↑ Pfahl, M (1972) Genetic map of the lactose repressor gene (i) of Escherichia coli. Genetics 72 393-410 PubMed OMPwiki page
  42. ↑ Weber, K et al. (1972) Altered sequences changing the operator-binding properties of the Lac repressor: colinearity of the repressor protein with the i-gene map. Proc. Natl. Acad. Sci. U.S.A. 69 3624-8 PubMed OMPwiki page
  43. ↑ Files, JG et al. (1974) Translational reinitiation: reinitiation of lac repressor fragments at three internal sites early in the lac i gene of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 71 667-70 PubMed OMPwiki page
  44. ↑ LESTER, G (1952) The beta-galactosidase of lactose mutants of Escherichia coli, K-12. Arch. Biochem. Biophys. 40 390-401 PubMed OMPwiki page
  45. ↑ APPEL, SH et al. (1965) MULTIPLE MOLECULAR FORMS OF BETA-GALACTOSIDASE. J. Mol. Biol. 11 12-22 PubMed OMPwiki page
  46. ↑ ALPERS, DH & TOMKINS, GM (1965) THE ORDER OF INDUCTION AND DEINDUCTION OF THE ENZYMES OF THE LACTOSE OPERON IN E. COLI. Proc. Natl. Acad. Sci. U.S.A. 53 797-802 PubMed OMPwiki page
  47. ↑ STEERS, E Jr et al. (1965) EVIDENCE FOR NONIDENTICAL CHAINS IN THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J. Biol. Chem. 240 2478-84 PubMed OMPwiki page
  48. ↑ Jayaraman, K et al. (1966) Inhibition of the synthesis of beta-galactosidase in Escherichia coli by 2-nitrophenyl-beta-D-fucoside. J. Mol. Biol. 18 339-43 PubMed OMPwiki page
  49. ↑ Grodzicker, T & Zipser, D (1968) A mutation which creates a new site for the re-initiation of polypeptide synthesis in the z gene of the lac operon of Escherichia coli. J. Mol. Biol. 38 305-14 PubMed OMPwiki page
  50. ↑ Fowler, AV & Zabin, I (1966) Co-linearity of beta-galactosidase with its gene by immunological detection of incomplete polypeptide chains. Science 154 1027-9 PubMed OMPwiki page
  51. ↑ Fowler, AV & Zabin, I (1966) Effects of Dimethylsulfoxide on the Lactose Operon in Escherichia coli. J. Bacteriol. 92 353-7 PubMed OMPwiki page
  52. ↑ Brown, JL et al. (1967) Beta-galactosidase: orientation and the carboxyl-terminal coding site in the gene. Proc. Natl. Acad. Sci. U.S.A. 58 1139-43 PubMed OMPwiki page
  53. ↑ Berg, AP et al. (1970) Beta-galactosidase: isolation of and antibodies to incomplete chains. J. Bacteriol. 101 438-43 PubMed OMPwiki page
  54. ↑ Villarejo, M et al. (1972) Beta-galactosidase. In vivo -complementation. J. Biol. Chem. 247 2212-6 PubMed OMPwiki page
  55. ↑ Zamenhof, PJ & Villarejo, M (1972) Construction and properties of Escherichia coli strains exhibiting -complementation of -galactosidase fragments in vivo. J. Bacteriol. 110 171-8 PubMed OMPwiki page
  56. ↑ Truman, P & Bergquist, PL (1976) Genetic and biochemical characterization of some missense mutations in the lacZ gene of Escherichia coli K-12. J. Bacteriol. 126 1063-74 PubMed OMPwiki page
  57. ↑ Langridge, J (1974) Genetic and enzymatic experiments relating to the quaternary structure of beta-galactosidase. Aust. J. Biol. Sci. 27 321-30 PubMed OMPwiki page
  58. ↑ Langridge, J (1974) Mutation spectra and the neutrality of mutations. Aust. J. Biol. Sci. 27 309-19 PubMed OMPwiki page
  59. ↑ Langridge, J (1968) Genetic and enzymatic experiments relating to the tertiary structure of beta-galactosidase. J. Bacteriol. 96 1711-7 PubMed OMPwiki page
  60. ↑ Langridge, J (1968) Genetic evidence for the disposition of the substrate binding site of beta-galactosidase. Proc. Natl. Acad. Sci. U.S.A. 60 1260-7 PubMed OMPwiki page
  61. ↑ Hobson, AC et al. (1977) Isolation, genetic analysis, and characterization of Escherichia coli mutants with defects in the lacY gene. J. Bacteriol. 131 830-8 PubMed OMPwiki page
  62. ↑ Carter, JR et al. (1968) Interaction of sugars with the membrane protein component of the lactose transport system of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 60 725-32 PubMed OMPwiki page
  63. ↑ Kusch, M & Wilson, TH (1973) Defective lactose utilization by a mutant of Escherichia coli energy-uncoupled for lactose transport. The advantages of active transport versus facilitated diffusion. Biochim. Biophys. Acta 311 109-22 PubMed OMPwiki page
  64. ↑ Wilson, TH et al. (1970) A mutant in Escherichia coli energy-uncoupled for lactose transporta defect in the lactose-operon. Biochem. Biophys. Res. Commun. 40 1409-14 PubMed OMPwiki page
  65. ↑ Fox, CF & Kennedy, EP (1965) Specific labeling and partial purification of the M protein, a component of the beta-galactoside transport system of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 54 891-9 PubMed OMPwiki page
  66. ↑ Fox, CF et al. (1967) GENETIC CONTROL OF THE MEMBRANE PROTEIN COMPONENT OF THE LACTOSE TRANSPORT SYSTEM OF Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 57 698-705 PubMed OMPwiki page
  67. ↑ Kennedy, EP et al. (1974) Dierect measurement of the binding of labeled sugars to the lactose permease M protein. J. Biol. Chem. 249 33-7 PubMed OMPwiki page
  68. ↑ Del Piano, M () [Importance of active and passive anti-rubella immunoprophylaxis]. Nuovi Ann Ig Microbiol 30 404-20 PubMed OMPwiki page
  69. ↑ ZABIN, I et al. (1962) Thiogalactoside transacetylase. J. Biol. Chem. 237 253-7 PubMed OMPwiki page
  70. ↑ Fox, CF et al. (1966) Transposition of the lac region of Escherichia coli. II. On the role of thiogalactoside transacetylase in lactose metabolism. J. Mol. Biol. 19 576-9 PubMed OMPwiki page
  71. ↑ Musso, RE & Zabin, I (1973) Substrate specificity and kinetic studies on thiogalactoside transacetylase. Biochemistry 12 553-7 PubMed OMPwiki page
  72. ↑ Brown, JL et al. (1967) Thiogalactoside transacetylase. Amino- and carboxyl-terminal studies. J. Biol. Chem. 242 4259-62 PubMed OMPwiki page
  73. ↑ Brown, JL et al. (1967) Thiogalactoside transacetylase. Physical and chemical studies of subunit structure. J. Biol. Chem. 242 4254-8 PubMed OMPwiki page
  74. ↑ Andrews, KJ & Lin, EC (1976) Thiogalactoside transacetylase of the lactose operon as an enzyme for detoxification. J. Bacteriol. 128 510-3 PubMed OMPwiki page
  75. ↑ ALPERS, DH et al. (1965) A SPECTROPHOTOMETRIC ASSAY FOR THIOGALACTOSIDE TRANSACETYLASE. J. Biol. Chem. 240 10-3 PubMed OMPwiki page
  76. ↑ CRAVEN, GR et al. (1965) PURIFICATION, COMPOSITION, AND MOLECULAR WEIGHT OF THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J. Biol. Chem. 240 2468-77 PubMed OMPwiki page
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