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EcoSal Plus

Domain 1:

Historical Perspectives

and the French School of Molecular Biology

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  • Author: Agnes Ullmann1
  • Editor: James B. Kaper2
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Institut Pasteur, 75015 Paris, France; 2: University of Maryland, School of Medicine, Baltimore, MD
  • Received 09 October 2009 Accepted 09 December 2009 Published 25 January 2010
  • Address correspondence to Agnes Ullmann [email protected]
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  • Abstract:

    André Lwoff, Jacques Monod, and François Jacob, the leaders of the French school of molecular biology, greatly contributed between 1937 and 1965 to its development and triumph. The main discovery of Lwoff was the elucidation of the mechanism of bacteriophage induction, the phenomenon of lysogeny, that led to the model of genetic regulation uncovered later by Jacob and Monod. Working on bacterial growth, Monod discovered in 1941 the phenomenon of diauxy and uncovered the nature of enzyme induction. By combining genetic and biochemical approaches, Monod brought to light the structure and functions of the lactose system, comprising the genes necessary for lactose metabolism, i.e., β-galactosidase and lactose permease, a pump responsible for accumulation of galactosides into the cells. An additional genetic factor (the gene) determines the inducibility and constitutivity of enzyme synthesis. Around the same time, François Jacob and Elie Wollman dissected the main events of bacterial conjugation that enabled them to construct a map of the chromosome and to demonstrate its circularity. The genetic analysis of the lactose system led Monod and Jacob to elucidate the mechanism of the regulation of gene expression and to propose the operon model: a unit of coordinate transcription. One of the new concepts that emerged from the operon model was messenger RNA. In 1963, Monod developed one of the most elegant concepts of molecular biology, the theory of allostery. In 1965, Lwoff, Monod and Jacob were awarded the Nobel Prize in Physiology or Medicine.

  • Citation: Ullmann A. 2010. and the French School of Molecular Biology, EcoSal Plus 2010; doi:10.1128/ecosalplus.1.1.1

References

1. Beadle GW, Tatum EL. 1941. Genetic control of biochemical reactions in Neurospora. Proc Natl Acad Sci USA 27:499–506. [PubMed][CrossRef]
2. Morange M. 2004. A History of Molecular Biology, p 43–47. Harvard University Press, Cambridge, MA.
3. Monod J. 1966. From enzymatic adaptation to allosteric transitions (Nobel Lecture). Science 154:1475–1483. [PubMed][CrossRef]
4. Luria SE, Delbrück M. 1943. Mutations of bacteria from virus sensitivity to virus resistance. Genetics 28:491–511.[PubMed]
5. Avery OT, MacLeod CM, McCarthy M. 1944. Studies of the chemical nature of the substance inducing transformation of pneumococcal types. Induction of transformation by a deoxyribonucleic acid fraction isolated from pneumococcus type III. J Exp Med 89:137–158. [CrossRef]
6. Judson HF. 1996. The Eighth Day of Creation, p 37. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
7. Lwoff A. 1932. Recherches Biochimiques sur la Nutrition des Protozoaires. Masson ed., Paris, France.
8. Lwoff A. 1944. L’Evolution Physiologique: Etude des Pertes de Fonctions chez les Microorganismes. Hermann ed., Paris, France.
9. Lwoff A. 1971. From protozoa to bacteria and viruses. Fifty years with microbes. Ann Rev Microbiol 25:1–26. [PubMed][CrossRef]
10. Monod J. 1941. Sur un phénomène nouveau de croissance complexe dans les cultures bactériennes. C R Acad Sci (Paris) 212:934–936.
11. Monod J. 1942. Recherche sur la croissance des cultures bactériennes. Doctoral thesis. Hermann ed., Paris, France.
12. Magasanik B. 1961. Catabolite repression. Cold Spring Harbor Symp Quant Biol 26:249–256.
13. Cohn M, Monod J. 1953. Specific inhibition and induction of enzyme biosynthesis, p 132–149. In “Adaptation in Microorganisms” London Symposium. Cambridge University Press, Cambridge, United Kingdom.
14. Hogness DS, Cohn M, Monod J. 1955. Studies on induced synthesis of β-galactosidase in Escherichia coli: the kinetics and mechanism of sulfur incorporation. Biochim Biophys Acta 16:99–116. [PubMed][CrossRef]
15. Monod J, Pappenheimer AM, Jr, Cohen-Bazire G. 1952. La cinétique de la biosynthèse de la β-galactosidase chez Escherichia coli considérée comme fonction de la croissance. Biochim Biophys Acta 9:648–660. [PubMed][CrossRef]
16. Monod J, Cohn M. 1952. La biosynthèse induite des enzymes (adaptation enzymatique). Adv Enzymol 13:67–119.
17. Cohn M, Monod J, Pollock MR, Spiegelman S, Stanier RY. 1953. Terminology of enzyme formation. Nature 172:1096. [PubMed][CrossRef]
18. Rickenberg H, Cohen GN, Buttin G, Monod J. 1956. La galactoside—perméase d’ Escherichia coli. Ann Inst Pasteur 91:829–857.
19. Büchel DE, Gronenborn B, Müller-Hill B. 1980. Sequence of the lactose permease gene. Nature 283:541–545. [PubMed][CrossRef]
20. Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S. 2003. Structure and mechanism of the lactose permease of Escherichia coli. Science 301:610–615. [PubMed][CrossRef]
21. Jacob F, Monod J. 1959. Gènes de structure et gènes de régulation dans la biosynthèse des protéines. C R Acad Sci 249:1282–1284.
22. Zabin I, Kepes A, Monod J. 1959. On the enzymatic acetylation of isopropyl-β- D-thiogalactoside and its association with galactoside-permease. Biochem Biophys Res Commun 1:289–292. [CrossRef]
23. Lwoff A. 1966. The prophage and I, p 88–99. In Cairns J, Stent GS, and Watson JD (ed), Phage and the Origins of Molecular Biology. Cold Spring Harbor Laboratory of Quantitative Biology, Cold Spring Harbor, NY.
24. Lwoff A. 1953. Lysogeny. Bacteriol Rev 17:269–337.[PubMed]
25. Lwoff A, Gutmann A. 1950. Recherches sur un Bacillus megatherium lysogène. Ann Inst Pasteur 78:711–739.
26. Lederberg J, Tatum E. 1946. Gene recombination in E. coli. Nature 158:558. [CrossRef]
27. Cavalli LL, Lederberg J, Lederberg E. 1953. An infecting factor controlling sex compatibility in Bacterium coli. J Gen Microbiol 8:89–103.[PubMed]
28. Hayes W. 1953. The mechanism of genetic recombination in Escherichia coli. Cold Spring Harbor Symp Quant Biol 26:386–401.
29. Lederberg EM, Lederberg J. 1953. Genetic studies of lysogenicity in Escherichia coli. Genetics 38:51–64.[PubMed]
30. Wollman EL. 1953. Sur le détérminisme génétique de la lysogénie. Ann Inst Pasteur 84:281–293.
31. Jacob F, Wollman E. 1956. Sur les processus de conjugaison et de recombinaison chez Escherichia coli: l'induction par conjugaison ou induction zygotique. Ann Inst Pasteur 91:486–510.
32. Jacob F, Wollman EL. 1957. Genetic aspects of lysogeny, p 468–500. In McElroy WD and Glass B (ed), The Chemical Basis of Heredity. The Johns Hopkins University Press, Baltimore, MD.
33. Wollman EL, Jacob F. 1955. Sur le mécanisme de transfert de matériel génétique au cours de la recombinaison chez Escherichia coli K12. C R Acad Sci 240:2449–2451.
34. Jacob F, Wollman EL. 1961. Sexuality and the Genetics of Bacteria. Academic Press, New York, NY.
35. Jacob F, Wollman E. 1958. Les épisomes, elements génétiques ajoutés. C R Acad Sci 247:154–156.
36. Pardee AB, Jacob F, Monod J. 1959. The genetic control and cytoplasmic expression of “inducibility” in the synthesis of β-galactosidase in Escherichia coli. J Mol Biol 1:165–178. [CrossRef]
37. Jacob F, Monod J. 1961. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol 3:318–356. [PubMed][CrossRef]
38. Jacob F, Monod J. 1961. On the regulation of gene activity. Cold Spring Harbor Symp Quant Biol 26:193–211.
39. Jacob F, Monod J. 1961. Teleonomic mechanisms in cellular metabolism, growth and differentiation. Cold Spring Harbor Symp Quant Biol 26:386–401.
40. Jacob F, Ullmann A, Monod J. 1964. Le promoteur, élément génétique nécessaire à l'expression d'un opéron. C R Acad Sci (Paris) 258:3125–3131.
41. Monod J, Changeux JP, Jacob F. 1963. Allosteric proteins and cellular control systems. J Mol Biol 6:306–329. [PubMed][CrossRef]
42. Monod J, Wyman J, Changeux J-P. 1965. On the nature of allosteric transitions: a plausible model. J Mol Biol 12:88–118. [PubMed][CrossRef]
43. Lwoff AM. 1977. Jacques Lucien Monod: 1910–1976, p 385–412. In Meade T (ed), Biographical Memoirs of Fellows of the Royal Society, vol. 23. Reprinted in A. Ullmann (ed), 2003, Origins of Molecular Biology: a Tribute to Jacques Monod, p 1–24. ASM Press, Washington, DC.
44. Lwoff A, Siminovitch L, Kjeldgaard N. 1950. Induction de la production de bacteriophages chez une bactérie lysogène. Ann Inst Pasteur 79:815–859.
1. Jacob F. 1988. The Statue within: an Autobiography. Basic Books, New York, NY.
2. Monod J, Borek E (ed). 1971. Of Microbes and Life. Columbia University Press, New York, NY.
3. Ullmann A (ed). 2003. Origins of Molecular Biology: a Tribute to Jacques Monod. ASM Press, Washington, DC.
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2010-01-25
2019-12-07

Abstract:

André Lwoff, Jacques Monod, and François Jacob, the leaders of the French school of molecular biology, greatly contributed between 1937 and 1965 to its development and triumph. The main discovery of Lwoff was the elucidation of the mechanism of bacteriophage induction, the phenomenon of lysogeny, that led to the model of genetic regulation uncovered later by Jacob and Monod. Working on bacterial growth, Monod discovered in 1941 the phenomenon of diauxy and uncovered the nature of enzyme induction. By combining genetic and biochemical approaches, Monod brought to light the structure and functions of the lactose system, comprising the genes necessary for lactose metabolism, i.e., β-galactosidase and lactose permease, a pump responsible for accumulation of galactosides into the cells. An additional genetic factor (the gene) determines the inducibility and constitutivity of enzyme synthesis. Around the same time, François Jacob and Elie Wollman dissected the main events of bacterial conjugation that enabled them to construct a map of the chromosome and to demonstrate its circularity. The genetic analysis of the lactose system led Monod and Jacob to elucidate the mechanism of the regulation of gene expression and to propose the operon model: a unit of coordinate transcription. One of the new concepts that emerged from the operon model was messenger RNA. In 1963, Monod developed one of the most elegant concepts of molecular biology, the theory of allostery. In 1965, Lwoff, Monod and Jacob were awarded the Nobel Prize in Physiology or Medicine.

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and the French School of Molecular Biology
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Citation: Ullmann A. 2010. and the French School of Molecular Biology, EcoSal Plus 2010; doi:10.1128/ecosalplus.1.1.1
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Figure 6

Growth of . in the presence of different carbohydrate pairs serving as the only source of carbon in a synthetic medium.

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Figure 6

Growth of . in the presence of different carbohydrate pairs serving as the only source of carbon in a synthetic medium.

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Figure 7

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Figure 7

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Figure 8

I, lactose: substrate of the enzyme, but deprived of inductive activity. II, methyl-β--galactoside: low-affinity substrate effective inducer. III, methyl-β--thiogalactoside: not hydrolyzable by the enzyme, but a powerful inducer. IV, phenyl-β--galactoside: excellent enzyme substrate, high affinity, no inductive ability. V, phenyl-β--thiogalactoside: no activity either as a substrate or as an inducer, but capable of acting as an antagonist of the inducer (from reference 3 ).

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Figure 8

I, lactose: substrate of the enzyme, but deprived of inductive activity. II, methyl-β--galactoside: low-affinity substrate effective inducer. III, methyl-β--thiogalactoside: not hydrolyzable by the enzyme, but a powerful inducer. IV, phenyl-β--galactoside: excellent enzyme substrate, high affinity, no inductive ability. V, phenyl-β--thiogalactoside: no activity either as a substrate or as an inducer, but capable of acting as an antagonist of the inducer (from reference 3 ).

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Figure 9

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Figure 9

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Figure 10

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Figure 10

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Figure 11

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Figure 12

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Figure 13

The lactose operon in the repressed (A) and induced state (B). In the absence of an inducer, the LacI repressor binds the operator and prevents gene expression, while in the presence of the inducer, the LacI repressor is inactivated and genes are expressed (drawing courtesy of Jean Marc Ghigo).

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Figure 13

The lactose operon in the repressed (A) and induced state (B). In the absence of an inducer, the LacI repressor binds the operator and prevents gene expression, while in the presence of the inducer, the LacI repressor is inactivated and genes are expressed (drawing courtesy of Jean Marc Ghigo).

Citation: Ullmann A. 2010. and the French School of Molecular Biology, EcoSal Plus 2010; doi:10.1128/ecosalplus.1.1.1
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Figure 14

In one of the two conformations, the protein can attach itself to the substrate and to the activating bond. In the other conformation, it can attach itself to the inhibiting bond (from reference 3 ).

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Figure 14

In one of the two conformations, the protein can attach itself to the substrate and to the activating bond. In the other conformation, it can attach itself to the inhibiting bond (from reference 3 ).

Citation: Ullmann A. 2010. and the French School of Molecular Biology, EcoSal Plus 2010; doi:10.1128/ecosalplus.1.1.1
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Figure 15

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Figure 15

Citation: Ullmann A. 2010. and the French School of Molecular Biology, EcoSal Plus 2010; doi:10.1128/ecosalplus.1.1.1
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