Control of the argECBH cluster in Escherichia coli
Tóm tắt
The argECBH genes in Escherichia coli are tightly clustered, but argE is not controlled coordinately with argCBH. Furthermore, while nonsense mutations have been isolated in argC and argB which are polar for argH, nonsense and frameshift mutations in argE are found nonpolar for the remaining genes in the cluster. Conditions have been realized for selecting mutations which relieve repression of argC without affecting control of arg genes outside the cluster. These mutations map between argE and argC, are cis-dominant, and cause partial constitutivity for argE as well as for argCBH. These results suggest that the argECBH cluster comprises two operons transcribed divergently from an internal operator-promoter complex.
Tài liệu tham khảo
Albrecht, A. M., Vogel, H. J.: Acetylornithine δ-transaminase. Partial purification and repression behavior. J. biol. Chem. 239, 1872–1876 (1964).
Baich, A., Vogel, H. J.: N-acetyl-γ-glutamokinase and N-acetylglutamic γ-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli. Biochem. biophys. Res. Commun. 7, 491–496 (1962).
Baumberg, S., Ashcroft, E.: Absence of polar effect of frameshift mutations in the E gene of the Escherichia coli argECBH cluster. J. gen. Microbiol. 69, 365–373 (1971).
Baumberg, S., Bacon, D. F., Vogel, H. J.: Individually repressible enzymes specified by clustered genes of arginine synthesis. Proc. nat. Acad. Sci. (Wash.) 53, 1029–1032 (1965).
Breckenridge, L., Gorini, L.: Genetic analysis of streptomycin resistance in Escherichia coli. Genetics 65, 9–25 (1970).
Clark, A. J.: Genetic analysis of a “double male” strain of Escherichia coli K-12. Genetics 48, 105–120 (1963).
Clark, A. J., Margulies, A. D.: Isolation and characterization of recombination-deficient mutants of Escherichia coli K12. Proc. nat. Acad. Sci. (Wash.) 53, 451–459 (1965).
Cunin, R., Elseviers, D., Sand, G., Freundlich, G., Glansdorff, N.: On the functional organization of the argECBH cluster of genes in Escherichia coli K-12. Molec. gen. Genet. 106, 32–47 (1969).
Cunin, R., Glansdorff, N.: Messenger RNA from arginine and phosphoenolpyruvate carboxylase genes in argR + and argR - strains of E. coli K-12. FEBS Letters 18, 135–137 (1971).
Davis, B. D., Mingioli, E. S.: Mutants of Escherichia coli requiring methionine or vitamin B12. J. Bact. 60, 17–28 (1950).
Elseviers, D., Cunin, R., Glansdorff, N., Baumberg, S., Ashcroft, E.: Organization of the argECBH cluster of genes in Escherichia coli K-12. Molec. gen. Genet., 117, 349–366 (1972).
Epstein, W., Davies, M.: Potassium-dependent mutants of Escherichia coli K-12. J. Bact. 101, 836–843 (1970).
Garrick-Silversmith, L., Hartman, P. E.: Histidine-requiring mutants of Escherichia coli K12, Genetic 66, 231–244 (1970).
Glansdorff, N.: Topography of cotransducible arginine mutations in Escherichia coli K-12. Genetics 51, 167–179 (1965).
Glansdorff, N., Sand, G.: Coordination of enzyme synthesis in the arginine pathway of Escherichia coli K-12. Biochem. biophys. Acta (Amst.) 108, 308–311 (1965).
Gorini, L.: Regulation en retour (feedback control) de la synthèse de l'arginine chez Escherichia coli. Bull. Soc. Chim. biol. (Paris) 40, 1939–1952 (1958).
Gorini, L., Gundersen, W., Burger, M.: Genetics of regulation of enzyme synthesis in the arginine biosynthetic pathway of Escherichia coli. Cold Spr. Harb. Symp. quant. Biol. 26, 173–182 (1961).
Gorini, L., Kataja, E.: Phenotypic repair by streptomycin of defective genotypes in E. coli. Proc. nat. Acad. Sci. (Wash.) 51, 487–493 (1964).
Gorini, L., Kaufman, H.: Selecting bacterial mutants by the penicillin method. Science 131, 604–605 (1960).
Guha, A., Saturen, Y., Szybalski, W.: Divergent orientation of transcription from the biotin locus of Escherichia coli. J. molec. Biol. 56, 53–62 (1971).
Henning, U., Herz, C.: Ein Strukturgen-Komplex für den Pyruvat-dehydrogenase-Komplex von Escherichia coli K 12. Z. Vererbgsl. 95, 260–275 (1964).
Herbert, A. A., Guest, J. R.: Studies with α-ketoglutarate dehydrogenase mutants of Escherichia coli. Molec. gen. Genet. 105, 182–190 (1969).
Hirota, Y.: The effect of acridine dyes on mating type factors in Escherichia coli. Proc. nat. Acad. Sci. (Wash.) 46, 57–64 (1960).
Jacoby, G. A.: Mapping the gene determining ornithine transcarbamylase and its operator in Escherichia coli B. J. Bact. 108, 645–651 (1971).
Jacoby, G. A., Gorini, L.: Genetics of control of the arginine pathway in Escherichia coli B and K. J. molec. Biol. 24, 41–50 (1967).
Jacoby, G. A., Gorini, L.: A unitary account of the repression mechanism of arginine biosynthesis in Escherichia coli. I. The genetic evidence. J. molec. Biol. 39, 73–87 (1969).
Karlström, O., Gorini, L.: A unitary account of the repression mechanism of arginine biosynthesis in Escherichia coli. II. Application to the physiological evidence. J. molec. Biol. 39, 89–94 (1969).
Krzyzek, R., Rogers, P.: Arginine control of transcription of argECBH messenger ribonucleic acid in Escherichia coli. J. Bact. 110, 945–954 (1972).
Lavallé, R.: Regulation at the level of translation in the arginine pathway of Escherichia coli K12. J. molec. Biol. 51, 449–451 (1970).
Lennox, E. S.: Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1, 190–206 (1955).
Levinthal, M., Nikaido, H.: Consequences of deletion mutations joining two operons of opposite polarity. J. molec. Biol. 42, 511–520 (1969).
Low, B.: Formation of merodiploids in matings with a class of rec- recipient strains of Escherichia coli K12. Proc. nat. Acad. Sci. (Wash.) 60, 160–167 (1968).
Lowry, O. H., Rosenbrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the folin phenol reagent. J. biol. Chem. 193, 265–275 (1951).
Maas, W.: Studies on repression of arginine biosynthesis in Escherichia coli. Cold. Spr. Harb. Symp. quant. Biol. 26, 183–191 (1961).
McLellan, W. L., Vogel, H. J.: Translational repression in the arginine system of Escherichia coli. Proc. nat. Acad. Sci. (Wash.) 67, 1703–1709 (1970).
Newton, W. A., Beckwith, J. R., Zipser, D., Brenner, S.: Nonsense mutants and polarity in the lac operon of Escherichia coli. J. molec. Biol. 14, 290–296 (1965).
Pittard, J., Loutit, J. S., Adleberg, E. A.: Gene transfer by F′ strains of Escherichia coli K-12. J. Bact. 85, 1394–1401 (1963).
Ratner, S., Anslow, W. P., Jr., Petrack, B.: Biosynthesis of urea. VI. Enzymatic cleavage of argininosuccinic acid to arginine and fumaric acid. J. biol. Chem. 204, 115–125 (1953).
Reznikoff, W. S., Miller, J. H., Scaife, J. G., Beckwith, J. R.: A mechanism for repressor action. J. molec. Biol. 43, 201–213 (1969).
Rogers, P., Krzyzek, R., Kaden, T. M., Arfman, E.: Effect of arginine and canavanine on arginine messenger RNA synthesis. Biochem. biophys. Res. Commun. 44, 1220–1226 (1971).
Sanderson, K. E.: Current linkage map of Salmonella typhimurium. Bact. Rev. 34, 176–193 (1970).
Stacey, K. A., Simson, E.: Improved method for the isolation of thymine-requiring mutants of Escherichia coli. J. Bact. 90, 554–555 (1965).
Steinberg, C. M., Edgar, R. S.: A critical test of a current theory of genetic recombination in bacteriophage. Genetics 47, 187–208 (1962).
Strigini, P., Gorini, L.: Ribosomal mutations affecting efficiency of amber suppression. J. molec. Biol. 47, 517–530 (1970).
Taylor, A. L.: Current linkage map of Escherichia coli. Bact. Rev. 34, 155–175 (1970).
Vogel, H. J., Bonner, D. M.: Acetylornithinase of Escherichia coli: partial purification and some properties. J. biol. Chem. 218, 97–106 (1956).