Effect of DNA-interacting drugs on phage T7 RNA polymerase

• Autorzy: Piestrzeniewicz M. , Studzian K. , Wilmanska D. , Plucienniczak G. , Gniazdowski M.
• Języki publikacji: EN

Abstrakty

EN

9-Aminoacridine carboxamide derivatives studied here form with DNA intercalative complexes which differ in the kinetics of dissociation. Inhibition of total RNA synthesis catalyzed by phage T7 and Escherichia coli DNA-dependent RNA polymerases correlates with the formation of slowly dissociating acridine-DNA complex of time constant of 0.4-2.3 s. Their effect on RNA synthesis is compared with other ligands which form with DNA stable complexes of different steric properties. T7 RNA polymerase is more sensitive to distamycin A and netropsin than the E. coli enzyme while less sensitive to actinomycin D. Actinomycin induces terminations in the transcript synthesized by T7 RNA polymerase. Despite low dissociation rates of DNA complexes with acridines and pyrrole antibiotics no drug dependent terminations are observed with these ligands.

Słowa kluczowe

EN

acridine; transcription; pyrrole antibiotic; actinomycin D; netropsin; RNA synthesis; Escherichia coli; inhibition; distamycin; RNA polymerase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1998
• Tom: 45
• Numer: 1
• Opis fizyczny: p.127-132,fig.

Twórcy

autor

Piestrzeniewicz M.

• Medical University in Lodz, W.Lindleya 6, 90-131 Lodz, Poland, E-mail: [e-mail]

autor

Studzian K.

autor

Wilmanska D.

autor

Plucienniczak G.

autor

Gniazdowski M.

Bibliografia

• 1. Richardson, J.P. (1973) J. Moi BioL 78. 703-714.
• 2. Sarris, A.M., Niles, E.G. & Canellakis, E.S. (1977) Biochim. Biophys. Acta 474, 268-278.
• 3. Geacintov, N.E., Waldmeyer, I., Kuzmin, V.A. & Kolubayev, T. (1981) J. Phys. Chem. 85, 3608-3613.
• 4. Straney, D.C. & Crothers, D.M. (1987) Bio­chemistry 26, 1987-1995.
• 5. Mirau, P.A. & Shafer, R.H. (1982) Biochemis­try- 21, 2626-2631.
• 6. Gale, E.F., Cundliffe, E., Reynold«, P.E., Rich­mond, M.H. & Waring, M.J. (1981) in: The Molecular Basis of Antibiotic Action, pp. 258-401, J. Wiley, New York.
• 7. Wakelin, L.P.G., Atwell, G.J., Rewcastle, G.W. & Denny, W.A. (1987) J. Med. Chem. 30, 855-861.
• 8. Piestrzeniewicz, M., Czyż, M., Denny, W.A. & Gniazdowski, M. (1990) Acta Biochim. Polon. 37, 299-307.
• 9. Piestrzeniewicz, M., Wilmańska. D., Studzian, K., Szemraj, J., Czyż, M., Denny, W.A. & Gni­azdowski, M., Z. Naturforsch. in press.
• 10. Tabor, S. & Richardson, C.C. (1985) Proc. Natl. Acad. Sci. U.S.A 82, 1074-1078.
• 11. Evans, C.T., Owens, D.D., Sumegi, B., Kispal, G. & Srere, P.A. (1988) Biochemistry 27, 4680-4686.
• 12. Halle well, R.A., Masiarz, F.R., Najarian, R.C., Puma, J.P., Quiroga, M.R., Randolph, A., Sanchez-Pescador, R., Scandella, C.J., Smith, B.f Steimer, K.S. & Mullenbach, G.T. (1985) Nucleic Acids Res. 13, 2017-2034.
• 13. Sherman, L., Dafni, N., Lieman-Hurwitz, J. & Groner, Y. (1983) Proc. Natl. Acad. Sci. U.S.A. 80,5465-5469.
• 14. Jaros-Kam:ńska, B., Małagocka, E., Ciesiel­ska, E. & Gniazdowski, M. (1981) Stud. Bio- phys. 86, 211-218.
• 15. Krey. A.K., Allison, R.G. & Hahn, F.E. (1973) FEBS Lett 29, 58-62.
• 16. Küpper, K.A., McAllister, W.T. & Bautz, E.K.F. (1973) Eur. J. Biochem. 38, 581-586.
• 17. White, R.J. & Phillips, D.R. (1989) Biochemis­try 28, 4277-4282.
• 18. Portugal. J. (1995) Anti-Cancer Drug Design 10, 427-438.
• 19. Puschendorf, B., Petersen, E., Wolf, H., Wer- chau, H. & Grunicke, H. (1971) Biochem. Bio- phys. Res. Commun. 43, 617-624.
• 20. Gniazdowski, M. & Cera, C. (1996) Chem. Rev. 96. 619-634.