1887

Chapter 15 : Carbon Source-Mediated Catabolite Repression

Author: Glenn H. Chambliss1
VIEW AFFILIATIONS HIDE AFFILIATIONS
Affiliations: 1: Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin 53706
Content Type: Monograph
Publication Year: 1993

Category: Bacterial Pathogenesis; Microbial Genetics and Molecular Biology

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Preview this chapter:
Preview Magnify
Zoom in
Zoomout

Carbon Source-Mediated Catabolite Repression, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555818388/9781555810535_Chap15-1.gif /docserver/preview/fulltext/10.1128/9781555818388/9781555810535_Chap15-2.gif

Abstract:

Catabolite repression is a regulatory mechanism by which the cell (i) coordinates metabolism of carbon a n d energy sources to maximize efficiency and (ii) regulates other metabolic processes as well. The objective of this review is to examine what is known about the molecular mechanisms by which catabolite repression operates in gram-positive bacteria, especially . In this chapter, the author uses the term catabolite repression to refer specifically to carbon source-mediated regulation and not to regulation by nitrogen or other nutrient sources. The phenomenon of catabolite repression has been best characterized in . The chapter briefly reviews the basic mechanism by which accomplishes the type of global regulation. Catabolite repression in is interference with a positive regulatory mechanism in which the catabolite repressor protein (CRP or CAP) in complex with the cyclic nucleotide cyclic AMP (cAMP) binds to a specific site in the promoter region of catabolite repression-sensitive genes or operons. In the three genera of gram-positive bacteria (), the molecular mechanism by which catabolite repression functions appears to be fundamentally different from that in . To date, few studies have been directed at elucidating the molecular mechanism by which carbon source-mediated catabolite repression operates. The mechanism by which monitors its environment for the presence of readily metabolized carbohydrates and translates that information into regulatory signals is unknown.

Citation: Chambliss G. 1993. Carbon Source-Mediated Catabolite Repression, p 213-219. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch15

Key Concept Ranking

Transcription Start Site
0.50532305
CcpA Repressor
0.4126066
0.50532305
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

References

/content/book/10.1128/9781555818388.chap15
1. Adler, K.,, K. Beyreuther,, E. Fanning,, N. Geisler,, B. Gronenborn,, A. Klemm,, B. Muller-Hlll,, M. Pfahl,, and A. Schmitz. 1972. How lac repressor binds to DNA. Nature (London) 237: 322– 327.
2. Bjorklind, A.,, and S. Arvidson. 1980. Mutants of Staphylococcus aureus affected in the regulation of exoprotein synthesis. FEMS Microbiol. Lett. 7: 203– 206.
3. Buttner, M. J.,, A. M. Smith,, and M. J. Bibb. 1988. At least three different RNA polymerase holoenzymes direct transcription of the agarase gene (dagA) of Streptomyces coelicolor A3(2). Cell 52: 599– 609.
4. Champness, W. 1988. New loci required for Streptomyces coelicolor morphological and physiological differentiation. J. Bacteriol. 170: 1168– 1174.
5. Chater, K. F., 1984. Morphological and physiological differentiation in Streptomyces, p. 89– 115. In R. Losick, and L. Shapiro (éd.), Microbial Development. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y..
6. Chatterjee, S.,, and L. C. Vining. 1982. Catabolite repression in Streptomyces venezuelae. Induction of β-galactosidase, chloramphenicol production, and intracellular cyclic adenosine 3',5' monophosphate concentrations. Can. J. Microbiol. 28: 311– 317.
7. Delic, I.,, P. Robbins,, and J. Westphellng. 1992. Direct repeat sequences are implicated in the regulation of two chitinase promoters that are subject to carbon catabolite control in Streptomyces. Proc. Natl. Acad. Sci. USA 89: 1885– 1889.
8. Doi, R. H.,, M. Gitt,, L.-F. Wang,, C. W. Price,, and F. Kawamura,. 1985. Major sigma factor, sigma-43, of Bacillus subtilis RNA polymerase and interacting spoO products are implicated in catabolite control of sporulation, p. 157– 161. In J. Hoch, and P. Setlow (éd.), Molecular Biology of Microbial Differentiation. American Society for Microbiology, Washington, D.C..
9. Duncan, J. L.,, and G. J. Cho. 1972. Production of staphylococcal alpha toxin. II. Glucose repression of toxin formation. Infect. Immun. 6: 689– 694.
10. Ebright, R. H., 1986. Proposed amino acid-base pair contacts for 13 sequence-specific DNA binding proteins, p. 207– 219. In D. L. Oxender (éd.), Protein Structure, Folding, and Design. Alan R. Liss, Inc., New York.
11. Epps, H. M. R.,, and E. F. Gale. 1942. The influence of the presence of glucose during growth on the enzymic activities of Escherichia coli: comparison of the effect with that produced by fermentation acids. Biochem. J. 36: 619– 623.
11a.. Fisher, S. Personal communication.
12. Fisher, S. H.,, and A. L. Sonenshein. 1991. Control of carbon and nitrogen metabolism in Bacillus subtilis. Annu. Rev. Microbiol. 43: 107– 135.
13. Fornwald, J. A.,, F. J. Schmidt,, C. W. Adams,, M. Rosenberg,, and M. E. Brawner. 1987. Two promoters, one inducible and one constitutive, control transcription of the Streptomyces lividans galactose operon. Proc. Natl. Acad. Sci. USA 84: 2130– 2134.
14. Fouet, A.,, and A. L. Sonenshein. 1990. A target for carbon source-dependent negative regulation of the citB promoter of Bacillus subtilis. J. Bacteriol. 172: 835– 844.
15. Gaskill, M. E.,, and S. A. Khan. 1988. Regulation of the enterotoxin B gene in Staphylococcus aureus. J. Biol. Chem. 263: 6276– 6280.
16. Gilman, M. Z.,, R. N. Wilson,, and R. A. Weinberg. 1986. Multiple protein binding sites in the 5'-flanking region regulate c-fos expression. Mol. Cell. Biol. 6: 4305– 4316.
17. Gordon, A. J. E.,, P. A. Burns,, D. F. Fy,, F. Yatagi,, F. L. Allen,, M. J. Horsfall,, J. A. Halliday,, J. Gray,, C. Bernelot-Moens,, and B. W. Glickman. 1988. Missense mutation in the lad gene of Escherichia coli. Inferences on the structure of the repressor protein. J. Mol. Biol. 200: 239– 251.
18. Hanson, R. S.,, J. A. Peterson,, and A. A. Yousten. 1970. Unique biochemical events in bacterial sporulation. Annu. Rev. Microbiol. 24: 53– 90.
19. Henkln, T. M.,, F. J. Grundy,, W. L. Nicholson,, and G. H. Chambliss. 1991. Catabolite repression of an amylase gene expression in Bacillus subtilis involves a transacting gene product homologous to and galR repressors. Mol. Microbiol. 5: 575– 584.
20. Hodgson, D. A. 1980. Carbohydrate utilization in Streptomyces coelicolor A3(2). Ph.D. thesis, University of East Anglia, Norwich, United Kingdom.
21. Hodgson, D. A. 1982. Glucose repression of carbon source uptake in Streptomyces coelicolor A3(2) and its perturbation in mutants resistant to 2-deoxyglucose. J. Gen. Microbiol. 128: 2417– 2430.
22. landolo, J. J.,, and W. J. Shafer. 1977. Regulation of staphylococcal enterotoxin B. Infect. Immun. 16: 610– 616.
23. Ide, M. 1971. Adenylcyclase of bacteria. Arch. Biochem. Biophys. 144: 262– 268.
24. Ikeda, H.,, E. T. Seno,, C. J. Bruton,, and K. F. Chater. 1984. Genetic mapping, cloning and physiological aspects of the glucose kinase gene of Streptomyces coelicolor. Mol. Gen. Genet. 196: 501– 507.
25. Ingram, C.,, M. Brawner,, P. Youngman,, and J. Westpheling. 1989. xylE functions as an efficient reporter gene in Streptomyces spp.: use for the study of galPl, a catabolite-controlled promoter. J. Bacteriol. 171: 6617– 6624.
26. Irani, M.,, L. Orosz,, S. Busby,, T. Tanlguchl,, and S. Adhya. 1983. Cyclic AMP-dependent constitutive expression of gal operon: use of repressor titration to isolate operator mutations. Proc. Natl. Acad. Sci. USA 80: 4775– 4779.
27. Jacob, S.,, R. Allmansberger,, D. Gartner,, and W. Hillen. 1991. Catabolite repression of the operon for xylose utilization from Bacillus subtilis W23 is mediated at the level of transcription and depends on a cis site in thexylA reading frame. Mol. Gen. Genet. 229: 189– 196.
28. Jarvls, A. W.,, R. C. Lawrence,, and G. G. Pritchard. 1975. Glucose repression of enterotoxins A, B and C and other extracellular proteins in staphylococci in batch and continuous culture. J. Gen. Microbiol. 86: 75– 87.
29. Kleina, L. G.,, and J. H. Miller. 1990. Genetic studies of the lac repressor. XIII. Extensive amino acid replacements generated by the use of natural and synthetic suppressors. J. Mol. Biol. 212: 295– 318.
30. Magasanlk, B. 1961. Catabolite repression. Cold Spring Harbor Symp. Quant. Biol. 26: 249– 256.
31. Magasanlk, B., 1970. Glucose effects: inducer exclusion and repression, p. 189– 219. In J. R. Beckwith, and D. Zipser (éd.). The Lactose Operon. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y..
32. Magasanlk, B.,, and F. C. Neidhardt,. 1987. Regulation of carbon and nitrogen utilization, p. 1318– 1325. In F. C. Neidhardt,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter,, and H. E. Umbarger (éd.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol. 2. American Society for Microbiology, Washington, D.C..
33. Maquat, L. E.,, K. Thornton,, and W. S. Reznikoff. 1980. lac promoter mutations located downstream from the transcription start site. J. Mol. Biol. 139: 537– 549.
34. Martin, I.,, M. Débarbouille,, A. Klier,, and G. Rapoport. 1989. Induction and metabolite regulation of levanase synthesis in Bacillus subtilis. J. Bacteriol. 171: 1885– 1892.
35. Martin, J. F.,, and A. L. Demain. 1980. Control of antibiotic biosynthesis. Microbiol. Rev. 44: 230– 251.
36. Miwa, Y.,, and Y. Fujlta. 1990. Determination of the cis sequence involved in catabolite repression of the Bacillus subtilis gnt operon; implication of a consensus sequence in catabolite repression in the genus Bacillus. Nucleic Acids Res. 18: 7049– 7053.
37. Miyashita, K.,, T. Fujii,, and Y. Sawada. 1991. Molecular cloning and characterization of chitinase genes from Streptomyces lividans 66. J. Gen. Microbiol. 137: 2065– 2072.
38. Monod, J. 1947. The phenomenon of enzymatic adaptation. Growth 11: 223– 289.
39. Nicholson, W. L. 1987. Regulation of α-amylase synthesis in Bacillus subtilis. Ph.D. thesis, University of Wisconsin, Madison.
40. Nicholson, W. L.,, and G. H. Chambliss. 1985. Isolation and characterization of a cis-acting mutation conferring catabolite resistance to α-amylase synthesis in Bacillus subtilis. J. Bacteriol. 161: 875– 881.
41. Nicholson, W. L.,, Y.-K. Park,, T. M. Henkln,, M. Won,, M. J. Welckert,, J. A. Gaskell,, and G. H. Chambliss. 1987. Catabolite repression-resistant mutations of the Bacillus subtilis alpha-amylase promoter affect transcription levels and are in an operator-like sequence. J. Mol. Biol. 198: 609– 618.
42. Oskouian, B.,,and G. C. Stewart. 1990. Repression and catabolite repression of the lactose operon of Staphylococcus aureus. J. Bacteriol. 172: 3804– 3812.
43. Postma, P. W., 1987. Phosphotransferase system for glucose and other sugars, p. 127– 141. In F. C. Neidhardt,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter,, and H. E. Umbarger (éd.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol. 2. American Society for Microbiology, Washington, D.C..
44. Regassa, L. B.,, J. L. Couch,, and M. J. Betley. 1991. Steady-state staphylococcal enterotoxin type C mRNA is affected by a product of the accessory gene regulator (agr) and by glucose. Infect. Immun. 59: 955– 962.
45. Sadler, J. R.,, H. Sasmor,, and J. L. Betz. 1983. A perfectly symmetric lac operator binds the lac repressor very tightly. Proc. Natl. Acad. Sci. USA 80: 6785– 6789.
46. Sauer, R. T.,, R. R. Yocum,, R. F. Doolittle,, M. Lewis,, and C. O. Pabo. 1982. Homology among DNA-binding proteins suggests use of a conserved super-secondary structure. Nature (London) 298: 447– 451.
47. Schaefler, P.,, J. Millet,, and J. D. Aubert. 1965. Catabolite repression of bacterial sporulation. Proc. Natl. Acad. Sci. USA 54: 704– 711.
48. Setlow, P. 1973. Inability to detect cyclic AMP in vegetative or sporulating cells or dormant spores of Bacillus megaterium. Biochem. Biophys. Res. Commun. 52: 365– 372.
49. Simons, A.,, D. Tib,, B. von Wilcken-Bergmann,, and B. Muller-Hlll. 1984. Possible ideal lac operator: Escherichia coli lac operator-like sequences from eukaryotic genomes lack the central G-C pair. Proc. Natl. Acad. Sci. USA 81: 1624– 1628.
50. Smith, C. P.,, and K. F. Chater. 1988. Cloning and transcriptional analysis of the entire glycerol utilization (glyABX) operon of Streptomyces coelicolor A3(2) and identification of a closely associated transcriptional unit. Mol. Gen. Genet. 211: 129– 137.
51. Smith, J. L.,, M. M. Bencivengo,, R. L. Buchanan,, and C. A. Kunsch. 1987. Effect of glucose analogs on the synthesis of staphylococcal enterotoxin A. J. Food Safety 8: 139– 146.
52. Smith, J. L.,, M. M. Bencivengo,, and C. A. Kunsch. 1986. Enterotoxin A synthesis in Staphylococcus aureus: inhibition by glycerol and maltose. J. Gen. Microbiol. 132: 3375– 3380.
53. Smith, T. F.,, and J. R. Sadler. 1971. The nature of lactose operator constitutive mutations. J. Mol. Biol. 59: 273– 305.
53a.. Stuhlkes, J. Personal communication.
54. Sun, D.,, and I. Takahashi. 1982. Genetic mapping of catabolite-resistant mutants of Bacillus subtilis. Can. J. Microbiol. 28: 1242– 1251.
55. Sun, D.,, and I. Takahashi. 1984. A catabolite-resistance mutation is localized in the rpo operon of Bacillus subtilis. Can. J. Microbiol. 30: 423– 429.
56. Takahashi, I. 1979. Catabolite repression-resistant mutants of Bacillus subtilis. Can. J. Microbiol. 25: 1283– 1287.
57. Ullmann, A.,, and A. Danchin. 1983. Role of cyclic AMP in bacteria. Adv. Cyclic Nucleotide Res. 15: 1– 53.
58. Vlrolle, M. J.,, and M. J. Bibb. 1988. Cloning, characterization and regulation of an alpha-amylase gene from Streptomyces limosus. Mol. Microbiol. 2: 197– 208.
59. von Wilcken-Bergmann, B.,, and B. Muller-Hill. 1982. Sequence of the galR gene indicates a common evolutionary origin of lac and gal repressor in Escherichia coli. Proc. Natl. Acad. Sci. USA 79: 2427– 2431.
60. Welckert, M.,, and S. Adhya. 1992. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 267: 15869– 15874.
61. Welckert, M.,, and G. Chambliss. 1990. Site-directed mutagenesis of a catabolite repression operator sequence in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 87: 6238– 6242.
62. Yamaguchl, K.,, H. Matsuzaki,, and B. Maruo. 1969. Participation of a regulator gene in the α-amylase production of Bacillus subtilis. J. Gen. Appl. Microbiol. 15: 97– 107.
63. Yamaguchl, K.,, Y. Nagata,, and B. Maruo. 1974. Genetic control of the rate of α-amylase synthesis in Bacillus subtilis. J. Bacteriol. 119: 410– 415.
64. Yuki, S. 1968. On the gene controlling the rate of α-amylase production in Bacillus subtilis. Biochem. Biophys. Res. Commun. 31: 182– 187.
65. Zahler, S. A.,, L. G. Benjamin,, B. S. Glatz,, P. F. Winter,, and B. J. Goldstein,. 1976. Genetic mapping of the alsA, alsR, thyA, kauA, and citD markers in Bacillus subtilis, p. 35– 43. In D. Schlessinger (éd.), Microbiology—1976. American Society for Microbiology, Washington, D.C..
66. Zahler, S. A.,, N. Najimudin,, D. S. Kessler,, and M. A. Vandeyar,. 1990. α-Acetolactate synthesis in Bacillus subtilis, p. 25– 42. In Z. Barak,, D. M. Chipman,, and J. V. Schloss (éd.), Biosynthesis of Branched Chain Amino Acids. VCH Verlagsgesellschaft, Berlin.

Back to top
This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error