Interaction of a Transcription Factor IIIA Peptide Containing Two Zinc Fingers with 5S rRNA

• Autorzy: Giel-Pietraszuk, M. , Mucha, P. , Rekowski, P. , Kupryszewski, G. , Barciszewska, M. Z.
• Języki publikacji: EN

Abstrakty

EN

The interaction of lupin ribosomal 5S RNA with a chemically synthesized peptide containing 60 amino acid, derived from Xenopus laevis transcription factor IIIA, is analyzed. The results show that such short fragment retains the ability of binding to 5S rRNA molecule, as shown by electrophoretic gel shift and RNase footprint assay. The peptide protects from hydrolysis with specific nucleases helix II and V of 5S rRNA.

Słowa kluczowe

EN

zinc finger peptide; transcription factor IIIA; Xenopus Laevis; ribosomal 5S RNA; protein-nucleic acid interaction

• Czasopismo: Polish Journal of Chemistry
• Rocznik: 2002
• Tom: Vol. 76 / nr 6
• Strony: 815-822
• Opis fizyczny: Bibliogr. 24 poz., rys.

Twórcy

autor

Giel-Pietraszuk, M.

• Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznań, Poland

autor

Mucha, P.

• Faculty of Chemistry, University of Gdańsk, Sobieskiego 18, 80-952 Gdańsk, Poland

autor

Rekowski, P.

• Faculty of Chemistry, University of Gdańsk, Sobieskiego 18, 80-952 Gdańsk, Poland

autor

Kupryszewski, G.

• Faculty of Chemistry, University of Gdańsk, Sobieskiego 18, 80-952 Gdańsk, Poland

autor

Barciszewska, M. Z.

• Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznań, Poland

Bibliografia

• 1. Mattaj I., Cell, 73, 837 (1993).
• 2. Miller J., McLachlan A.D. and Klug A., EMBO J., 4, 1609 (1985).
• 3. El-Baradi T. and Pieler T., Mech. Devel., 35, 155 (1991).
• 4. Engelke D.R., Ng S.Y., Shastry B.S. and Roeder R.G., Cell, 19, 717 (1980).
• 5. Pelham H.R.B. and Brown D.D., Proc. Natl. Acad. Sci. USA, 77, 4170 (1980).
• 6. Pavletich N.P. and Pabo C.O., Science, 252, 809 (1991).
• 7. Pavletich N.P. and Pabo C.O., Science, 261, 1701 (1993).
• 8. Elrod-Erickson M., Rould M.A., Nekludova L. and Pabo C.O., Structure, 4, 1171 (1996).
• 9. Nolte RT.,Conlin R.M., Harrison S.C. and Brown R.S., Proc. Natl. Acad. Sci. USA, 95,2938 (1998).
• 10. Foster M.P., Wuttke D.S., Radhakrishnan I., Case D.A., Gottesfeld J.M. and Wright P.E., Nat. Struct. Biol., A, 605(1997).
• 11. McBryant S.J., Veldhoen N., Gedulin B.,Leresche A. and Gottesfeld J.M., J. Mol. Biol., 248,44 (1995).
• 12. Theunissen O., Rudt F., Guddat U., Mentzel H. and Pieler T., Cell, 71, 679 (1992).
• 13. Clemens K.R., Wolf V., McBryant S. J., Zhang P., Liao X., Wright P.E. and Gottesfeld J.M., Science, 260, 530 (1993).
• 14. Setzer D.R., Menezes S.R, Del Rio S., Hung V.S. and Subramanyan G., RNA, 2, 1254 (1996).
• 15. Rollins M.B., Del Rio S., Galey A.L., Setzer D.R. and Andrews M., Mol. Cell. Biol., 313,4776 (1993).
• 16. Searles M.A. and Lu D., Klug A., J. Mol. Biol., 301, 47 (2000).
• 17. Hamilton T.B., Turner J., Barilla K. and Romaniuk P.J., Biochem., 40, 6093 (2001).
• 18. Frankel A.D., Berg J.N. and Pabo C.O., Proc. Natl. Acad. Sci. USA, 84, 4841 (1987).
• 19. Ellman G.L., Arch. Biochem. Biophys., 82, 70 (1957).
• 20. Riddles P.W. et al., Methods Enzymol., 91, 49 (1983).
• 21. Barciszewska M., Mashkova T.D., Zwierzyński T., Kisselev L.L. and Barciszewski J., Bull Acad. Polon. Sci., 34, 369 (1986).
• 22. Giel M., Slosarek G., Rekowski P., Kupryszewski G. and Barciszewski J., Int. J. Biol. Macromol., 15, 259(1993).
• 23. Friesen W.J. and Darby M.K., J. Biol. Chem., 276, 1968 (2001).
• 24. Ban N., Nissen P., Hansen J., Moore P.B. and Steitz T., Science, 289, 905 (2000).