Abstract
Genetic regulation is an essential function in all living organisms. In prokaryotes genetic control provides responsivity to a constantly changing external milieu, and bacterial systems have proved extremely valuable in elucidating the variety of potential mechanisms. Both positive and negative strategies exist for transcriptional control; this format for regulation at the initiation of mRNA synthesis allows maximum conservation of cellular energy. Positive control over a wide range of systems in E. coli is exerted by catabolite repression mediated by the CAP-cAMP system. Negative control in bacteria involves a series of repressor proteins, each specific for a particular pathway. Several of these systems and the details of their mechanisms of action will be discussed in this chapter.* The basic regulatory scheme involves the interaction of a repressor protein with its target DNA sequence in an inducibile or repressible manner (Fig. 6.1). Inducible mechanisms generally govern catabolic pathways where expression is necessary only in the presence of substrate. These genes are turned “off” through a repressor proteinoperator DNA interaction which interferes with transcription initiation by RNA polymerase. Derepression or induction is accomplished through destabilization of the repressor-operator complex upon binding of substrate, or a closely related inducer molecule, to the repressor protein. In contrast, repressible mechanisms most.often apply to biosynthetic pathways where gene expression is modulated by levels of the end product. To avoid overaccumulation, repression is established when the end product or related compound, acting as corepressor, binds to and activates an aporepressor protein. The resulting complex recognizes its cognate DNA sequence and thereby blocks transcription initiation.
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References
McKay, D.B., and Steitz, T.A. (1981) Nature 290, 144–749.
Anderson, J., Ptashne, M., and Harrison, S.C. (1984) Proc. Natl. Acad. Sci. USA 81, 1307–1311.
Anderson, W.F., Ohlendorf, D.H., Takeda, Y., and Matthews, B.W. (1981) Nature 290, 754–758.
Schevitz, R.W., Otwinowski, Z., Joachimiak, A., Lawson, C.L., and Sigler, P.B. (1985) Nature 317, 782–786.
Pabo, C.O., and Sauer, R.T. (1984) Annu. Rev. Biochem. 53, 293–321.
Ptashne, M. (1986) Nature 322, 697–701.
Schleif, R. (1988) Science 240, 127–128.
Weber, I.T., and Steitz, T.A. (1987) J. Mol. Biol. 198, 311–326.
Kolb, K., Spassky, A., Chapon, C., Blazy, B., and Buc, H. (1983) Nucleic Acids Res. 11, 7833–7852.
Liu-Johnson, H.N., Gartenberg, M.R., and Crothers, D.M. (1986) Cell 47, 995–1005.
Dripps, D., and Wartell, R.M. (1987) J. Biomol. Struct. Dynam. 5, 1–14.
Jacob, F., and Monod, J. (1961) J. Mol. Biol. 3, 318–356.
Miller, J.H., and Reznikoff, W.S. (eds.) (1980) The Operon. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
Barkley, M.D., Riggs, A.D., Jobe, A., and Bourgeois, S. (1975) Biochemistry 14, 1700–1712.
O’Gorman, R.B., Rosenberg, J.M., Kallai, O.B., Dickerson, R.E., Itakura, K., Riggs, A.D., and Matthews, K.S. (1980) J. Biol. Chem. 255, 10107–10114.
Daly, T.J., and Matthews, K.S. (1986) Biochemistry 25, 5479–5484.
Lin, S.-Y., and Riggs, A.D. (1975) Cell 4, 107–111.
Straney, S.B., and Crothers, D.M. (1987) Cell 57, 699–707.
Lohman, T.M. (1985) CRC Crit. Rev. Biochem. 19, 191–245.
Beyreuther, K., Adler, K., Fanning, E., Murray, C., Klemm, A., and Geisler, N. (1975) Eur. J. Biochem. 59, 491–509.
Farabaugh, P.J. (1978) Nature 274, 765–769.
Riggs, A.D., and Bourgeois, S. (1968) J. Mol. Biol. 34, 361–364.
Butler, A.P., Revzin, A., and Von Hippel, P.H. (1977) Biochemistry 16, 4757–4768.
Culard, F., and Maurizot, J.C. (1981) Nucleic Acids Res. 9, 5175–5184.
Whitson, P.A., and Matthews, K.S. (1986) Biochemistry 25, 3845–3852.
Platt, T., Files, J.G., and Weber, K. (1973) J. Biol. Chem. 248, 110–121.
Jovin, T.M., Geisler, N., and Weber, K. (1977) Nature 269, 668–672.
Kaptein, R., Zuiderweg, E.R.P., Scheek, R.M., Boelens, R., and Van Gunsteren, W.F. (1985) J. Mol. Biol. 182, 179–182.
Zuiderweg, E.R.P., Scheek, R.M., and Kaptein, R. (1985) Biopolymers 24, 2257–2277.
Steitz, T.A., Richmond, T.J., Wise, D., and Engelman, D. (1974) Proc. Natl. Acad. Sci. USA 71, 593–597.
Charlier, M., Maurizot, J.C., and Zaccai, G. (1981) J. Mol. Biol. 153, 177–182.
McKay, D.B., Pickover, C.A., and Steitz, T.A. (1982) J. Mol. Biol. 156, 175–183.
Pilz, I., Goral, K., Kratky, O., Bray, R.P., Wade-Jardetzky, N.G., and Jardetzky, O. (1980) Biochemistry 19, 4087–4090.
Wade-Jardetzky, N., Bray, R.P., Conover, W.W., Jardetzky, O., Geisler, N., and Weber, K. (1979) J. Mol. Biol. 128, 259–264.
Adler, K., Beyreuther, K., Fanning, E., Geisler, N., Gronenborn, B., Klemm, A., Müller-Hill, B., Pfahl, M., and Schmitz, A. (1972) Nature 237, 322–327.
Pfahl, M., Stockter, C., and Gronenborn, B. (1974) Genetics 76, 669–679.
Muller-Hill, B., Fanning, T., Geisler, N., Gho, D., Kania, J., Kathmann, P., Meissner, H., Schlotmann, M., Schmitz, A., Triesch, I., and Beyreuther, K. (1975) In Protein-Ligand Interactions, 211–227, Sund, H., and Blauer, G. (eds.). Walter de Gruyter and Co., Berlin.
Miller, J.H. (1979) J. Mol. Biol. 131, 249–258.
Miller, J.H. (1984) J. Mol. Biol. 180, 205–212.
Gordon, A.J.E., Burns, P.A., Fix, D.F., Yatagai, F., Allen, F.L., Horsfall, M.J., Halliday, J.A., Gray, J., Bernelot-Moens, C., and Glickman, B.W. (1988) J. Mol. Biol. 200, 239–251.
Ebright, R.H. (1986) Proc. Natl. Acad. Sci. USA 83, 303–307.
Lehming, N., Sartorius, J., Niemöller, M., Genenger, G., Von Wilcken-Bergmann, B., and Müller-Hill, B. (1987) EMBO J. 6, 3145–3153.
Friedman, B.E., and Matthews, K.S. (1978) Biochem. Biophys. Res. Commun. 85, 497–505.
Matthews, K.S. (1979) J. Biol. Chem 254, 3348–3353.
Manly, S.P., Bennett, G.N., and Matthews, K.S. (1984) J. Mol. Biol. 179, 335–350.
Geisler, N., and Weber, K. (1977) Biochemistry 16, 938–943.
Ogata, R.T., and Gilbert, W. (1979) J. Mol. Biol. 132, 709–728.
Culard, F., Schnarr, M., and Maurizot, J.C. (1982) EMBO J. 1, 1405–1409.
Nick, H., Arndt, K., Boschelli, F., Jarema, M.A.C., Lillis, M., Sadler, J., Caruthers, M., and Lu, P. (1982) Proc. Natl. Acad. Sci. USA 79, 218–222.
Schnarr, M., Durand, M., and Maurizot, J.C. (1983) Biochemistry 22, 3563–3570.
Barbier, B., Charlier, M., and Maurizot, J.C. (1984) Biochemistry 23, 2933–2939.
Boelens, R., Scheek, R.M., Van Boom, J.H., and Kaptein, R. (1987) J. Mol. Biol. 193, 213–216.
Daly, T.J., and Matthews, K.S. (1986) Biochemistry 25, 5474–5478.
Sams, C.F., Hemelt, V.B., Pinkerton, F.D., Schroepfer, G.J.S. Jr., and Matthews, K.S. (1985) J. Biol. Chem. 260, 1185–1191.
Muller-Hill, B. (1983) Nature 302, 163–164.
Sams, C.F., Vyas, N.K., Quiocho, F.A., and Matthews, K.S. (1984) Nature 310, 429–430.
Chakerian, A.E., Olson, J.S., and Matthews, K.S. (1987) Biochemistry 26, 7250–7255.
Smith, T.F., and Sadler, J.R. (1971) J. Mol. Biol. 59, 273–305.
Gilbert, W., Gralla, J., Majors, J., and Maxam, A. (1975) In Protein-Ligand Interactions, 193–210, Sund, H., and Blauer, G. (eds.). Walter de Gruyter and Co., Berlin.
Ogata, R., and Gilbert, W. (1977) Proc. Natl. Acad. Sci. USA 74, 4973–4976.
Schmitz, A., and Galas, D.J. (1979) Nucleic Acids. Res. 6, 111–137.
Manly, S.P., and Matthews, K.S. (1984) J. Mol. Biol. 179, 315–333.
Goeddel, D.V., Yansura, D.G., and Caruthers, M.H. (1978) Proc. Natl. Acad. Sci. USA 75, 3578–3582.
Caruthers, M.H., Beaucage, S.L., Efcavitch, J.W., Fisher, E.F., Goldman, R.A., De Haseth, P.L., Mandecki, W., Matteucci, M.D., Rosendahl, M.S., and Stabinsky, Y. (1982) Cold Spring Harbor Symp. Quant Biol. 47, 411–418.
Sadler, J.R., Sasmor, H., and Betz, J.L. (1983) Proc. Natl. Acad. Sci. USA 80, 6785–6789.
Simons, A., Tils, D., Von Wilcken-Bergmann, B., and Müller-Hill, B. (1984) Proc. Natl. Acad. Sci. USA 81, 1624–1628.
Reznikoff, W.S., Winter, R.B., and Hurley, C.K. (1974) Proc. Natl. Acad. Sci. USA 71, 2314–2318.
Pfahl, M., Guide, V., and Bourgeois, S. (1979) J. Mol. Biol. 127, 339–344.
Donnelly, C.E., and Reznikoff, W.S. (1987) J. Bacteriol. 169, 1812–1817.
Winter, R.B., and Von Hippel, P.H. (1981) Biochemistry 20, 6948–6960.
Hsieh, W.-T., Whitson, P.A., Matthews, K.S., and Wells, R.D. (1987) J. Biol. Chem 262, 14583–14591.
Whitson, P.A., Hsieh, W.-T., Wells, R.D., and Matthews, K.S. (1987) J. Biol. Chem. 262, 14592–14599.
Krämer, H., Amouyal, M., Nordheim, A., and Muller-Hill, B. (1988) EMBO J. 7, 547–556.
Krämer, H., Niemöller, M., Amouyal, M., Revet, B., Von Wilcken-Bergmann, B., and Müller-Hill, B. (1987) EMBO J. 6, 1481–1491.
Mossing, M.C., and Record, M.T. Jr. (1986) Science 233, 889–892.
Besse, M., Von Wilcken-Bergmann, B., and Müller-Hill, B. (1986) EMBO J. 5, 1377–1381.
Borowiec, J.A., Zhang, L., Sasse-Dwight, S., and Gralla, J.D. (1987) J. Mol. Biol. 196, 101–111.
Eismann, E., Von Wilcken-Bergmann, B., and Müller-Hill, B. (1987) J. Mol. Biol. 195, 949–952.
Dandanell, G., Valentin-Hansen, P., Larsen, J.E.L., and Hammer, K. (1987) Nature 325, 823–826.
Busby, S., Aiba, H., and De Crombrugghe, B. (1982) J. Mol. Biol. 154, 211–227.
Adhya, S., and Miller, W. (1979) Nature 279, 492–494.
Di Lauro, R., Taniguchi, T., Musso, R., and De Crombrugghe, B. (1979) Nature 279, 494–500.
Fritz, H.-J., Bicknäse, H., Gleumes, B., Heibach, C., Rosahl, S., and Ehring, R. (1983) EMBO J. 2, 2129–2135.
Irani, M.H., Orosz, L., and Adhya, S. (1983) Cell 32, 783–788.
Von Wilcken-Bergmann, B., Koenen, M., Griesser, H.W., and Müller-Hill, B. (1983) EMBO J. 2, 1271–1274.
Majumdar, A., and Adhya, S. (1984) Proc. Natl. Acad. Sci. USA 81, 6100–6104.
Von Wilcken-Bergmann, B., and Müller-Hill, B. (1982) Proc. Natl. Acad. Sci. USA 79, 2427–2431.
Majumdar, A., and Adhya, S. (1987) J. Biol. Chem 262, 13258–13262.
Musso, R., Di Lauro, R., Rosenberg, M., and De Crombrugghe, B. (1977) Proc. Natl. Acad. Sci. USA 74, 106–110.
Aiba, H., Adhya, S., and De Crombrugghe, B. (1981) J. Biol. Chem. 256, 11905–11910.
Irani, M.H., Orosz, L., Busby, S., Taniguchi, T., and Adhya, S. (1983) Proc. Natl. Acad. Sci. USA 80, 4775–4779.
Busby, S., Spassky, A., and Chan, B. (1987) Gene 53, 145–152.
Kuhnke, G., Krause, A., Heibach, C., Gieske, U., Fritz, H.-J., and Ehring, R. (1986) EMBO J. 5, 167–173.
Kuhnke, G., Fritz, H.-J., and Ehring, R. (1987) EMBO J. 6, 507–513.
Ponnambalam, S., Spassky, A., and Busby, S. (1987) FEBS Lett. 219, 189–196.
Shanblatt, S.H., and Revzin, A. (1983) Proc. Natl. Acad. Sci. USA 80, 1594–1598.
Lee, N. (1980) In The Operon, 389–409, Miller, J.H., and Reznikoff, W.S. (eds.). Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
Brunelle, A., Hendrickson, W., and Schleif, R. (1985) Nucleic Acids Res. 13, 5019–5026.
Cass, L.G., and Wilcox, G. (1986) J. Bacteriol. 166, 892–900.
Francklyn, C.S., and Lee, N. (1988) J. Biol. Chem. 263, 4400–4407.
Wilcox, G. (1974) J. Biol. Chem. 249, 6892–6894.
Lee, N., Francklyn, C., and Hamilton, E.P. (1987) Proc. Natl. Acad. Sci. USA 84, 8814–8818.
Hendrickson, W., and Schleif, R. (1985) Proc. Natl. Acad. Sci. USA 82, 3129–3133.
Martin, K., Huo, L., and Schleif, R.F. (1986) Proc. Natl. Acad. Sci. USA 83, 3654–3658.
Hamilton, E.P., and Lee, N. (1988) Proc. Natl. Acad. Sci. USA 85, 1749–1753.
Dunn, T.M., Hahn, S., Ogden, S., and Schleif, R.F. (1984) Proc. Natl. Acad. Sci. USA 81, 5017–5020.
Miyada, C.G., Stoltzfus, L., and Wilcox, G. (1984) Proc. Natl. Acad. Sci. USA 81, 4120–4124.
Hendrickson, W., and Schleif, R.F. (1984) J. Mol. Biol. 174, 611–628.
Bertrand, K.P., Postle, K., Wray, L.V. Jr., and Reznikoff, W.S. (1983) Gene 23, 149–156.
Wray, L.V. Jr., and Reznikoff, W.S. (1983) J. Bacteriol. 156, 1188–1191.
Hillen, W., Gatz, C., Altschmied, L., Schollmeier, K., and Meier, I. (1983) J. Mol. Biol. 169, 707–721.
Hansen, D., Altschmied, L., and Hillen, W. (1987) J. Biol. Chem. 262, 14030–14035.
Ball, P.R., Shales, S.W., and Chopra, I. (1980) Biochem. Biophys. Res. Commun. 93, 74–81.
McMurray, C., Petrucci, R.E. Jr., and Levy, S.B. (1980) Proc. Natl. Acad. Sci. USA 77, 3974–3977.
Isackson, P.J., and Bertrand, K.P. (1985) Proc. Natl. Acad. Sci. USA 82, 6226–6230.
Hansen, D., and Hillen, W. (1987) J. Biol. Chem. 262, 12269–12274.
Meier, I., Wray, L.V. Jr., and Hillen, W. (1988) EMBO J. 7, 567–572.
Wissmann, A., Meier, I., Wray, L.V. Jr., Geissendörfer, M., and Hillen, W. (1986) Nucleic Acids Res. 14, 4253–4266.
Gunsalus, R.P., and Yanofsky, C. (1980) Proc. Natl. Acad. Sci. USA 77, 7117–7121.
Horowitz, H., and Piatt, T. (1982) J. Mol. Biol. 156, 257–267.
Yanofsky, C. (1981) Nature 289, 751–758.
Singleton, C.K., Roeder, W.D., Bogosian, G., Somerville, R.L., and Weith, H.L. (1980) Nucleic Acids Res. 8, 1551–1560.
Lane, A.N., and Jardetzky, O. (1985) Eur. J. Biochem. 152, 405–409.
Lawson, C.L., Zhang, R., Schevitz, R.W., Otwinowski, Z., Joachimiak, A., and Sigler, P.B. (1988) Proteins 3, 18–31.
Zhang, R.-G., Joachimiak, A., Lawson, C.L., Schevitz, R.W., Otwinowski, Z., and Sigler, P.B. (1987) Nature 327, 591–597.
Tsapakos, M.J., Haydock, P.V., Hermodson, M., and Somerville, R.L. (1985) J. Biol. Chem. 260, 16383–16394.
Lane, A.N. (1986) Eur. J. Biochem. 157, 405–413.
Marmorstein, R.Q., Joachimiak, A., Sprinzl, M., and Sigler, P.B. (1987) J. Biol. Chem. 262, 4922–4927.
Arvidson, D.N., Bruce, C., and Gunsalus, R.P. (1986) J. Biol. Chem. 261, 238–243.
Joachimiak, A., Kelley, R.L., Gunsalus, R.P., Yanofsky, C., and Sigler, P.B. (1983) Proc. Natl. Acad. Sci. USA 80, 668–672.
Carey, J. (1988) Proc. Natl. Acad. Sci. USA 85, 975–979.
Rose, J.K., and Yanofsky, C. (1974) Proc. Natl. Acad. Sci. USA 71, 3134–3138.
Kelley, R.L., and Yanofsky, C. (1985) Proc. Natl. Acad. Sci. USA 82, 483–487.
Klig, L.S., Crawford, I.P., and Yanofsky, C. (1987) Nucleic Acids Res. 15, 5339–5351.
Kumamoto, A.A., Miller, W.G., and Gunsalus, R.P. (1987) Genes Dev. 1, 556–564.
Bass, S., Sugiono, P., Arvidson, D.N., Gunsalus, R.P., and Youderian, P. (1987) Genes Dev. 1, 565–572.
Flavin, M. (1975) In Metabolic Pathways, Vol. 7, 457–503, Greenberg, D.M. (ed.). Academic Press, New York.
Urbanowski, M.L., and Stauffer, G.V. (1985) Nucleic Acids Res. 13, 673–685.
Greene, R.C., Hunter, J.S.V., and Coch, E.H. (1973) J. Bacteriol. 115, 56–67.
Shoeman, R., Radfield, B., Coleman, T., Greene, R.C., Brot, N., and Weissbach, H. (1985) Proc. Natl. Acad. Sci. USA 82, 3601–3605.
Saint-Girons, I., Belfaiza, J., Guillou, Y., Perrin, D., Guiso, N., Bârzu, O., and Cohen, G.N. (1986) J. Biol. Chem. 261, 10936–10940.
Duchange, N., Zakin, M.M., Ferrara, P., Saint-Girons, I., Park, I., Tran, S.V., Py, M.-C., ańd Cohen, G.N. (1983) J. Biol. Chem. 258, 14868–14871.
Saint-Girons, I., Duchange, N., Zakin, M.M., Park, I., Margarita, D., Ferrarra, P., and Cohen, G.N. (1983) Nucleic Acids Res. 11, 6723–6732.
Belfaiza, J., Parsot, C., Martel, A., Bouthier de la Tour, C., Margarita, D., Cohen, G.N., and Saint-Girons, I. (1986) Proc. Natl. Acad. Sci. USA 83, 867–872.
Belfaiza, J., Guillou, Y., Margarita, D., Perrin, D., and Saint-Girons, I. (1987) J. Bacteriol. 169, 670–674.
Rafferty, J.B., Phillips, S.E.V., Rojas, C., Boulot, G., Saint-Girons, I., Guillou, Y., and Cohen, G.N. (1988) J. Mol. Biol. 200, 217–219.
Cunin, R., Glansdorff, N., Piérard, A., and Stalon, V. (1986) Microbiol. Rev. 50, 314–352.
Cunin, R., Eckhardt, T., Piette, J., Boyen, A., Piérard, A., and Glansdorff, N. (1983) Nucleic Acids Res. 11, 5007–5019.
Boyen, A., Charlier, D., Crabeel, M., Cunin, R., Palchaudhuri, S., and Glansdorff, N. (1978) Mol. Gen. Genet. 161, 185–196.
Lim, D., Oppenheim, J.D., Eckhardt, T., and Maas, W.K. (1987) Proc. Natl. Acad. Sci. USA 84, 6697–6701.
Hu, M.C.-T., and Davidson, N. (1988) Gene 62, 301–313.
Brown, M., Figge, J., Hansen, U., Wright, C., Jeang, K.-T., Khoury, G., Livingston, D.M., and Roberts, T.M. (1987) Cell 49, 603–612.
Figge, J., Wright, C., Collins, C.J., Roberts, T.M., and Livingston, D.M. (1988) Cell 52, 713–722.
Mukherjee, S., Erickson, H., and Bastia, D. (1988) Cell 52, 375–383.
Chao, M.V., Gralla, J.D., and Martinson, H.G. (1980) Biochemistry 19, 3254–3260.
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Wick, K.L., Matthews, K.S. (1989). Escherichia coli Repressor Proteins. In: Adolph, K.W. (eds) Molecular Biology of Chromosome Function. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3652-8_6
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