Sequences flanking rat hsp70.1 gene contain motifs specific for matrix attached regions and form complexes with nuclear matrix protein in vitro

• Autorzy: Widlak P. , Rogolinski J. , Lisowska K. , Rzeszowska-Wolny J.
• Języki publikacji: EN

Abstrakty

EN

Eukaryotic chromatin is organized into looped domains formed by attachment of specific DNA sequences (termed MARs or SARs) to network of nuclear proteins (nuclear matrix). We have looked for matrix attachments within 4.9 kb DNA region encompassing rat hsp70.1 gene. Sequences that flank both 3'-end and 5'-end of the gene contain motifs characteristic for MAR/SARs identified in numerous other genes. These flanking sequences formed in vitro complexes with proteins of the nuclear matrix from different rat tissues. Using Southwestern analysis we showed that similar matrix proteins interacted with sequences flanking rat hsp70.1 gene and established MAR from mouse kappa immunoglobulin gene.

Słowa kluczowe

EN

DNA sequence; mouse; mice; eukaryotic chromatin; heat shock gene; protein; nuclear matrix; in vitro; rat; tissue

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 1997
• Tom: 02
• Numer: 3
• Opis fizyczny: p.317-324,fig.

Twórcy

autor

Widlak P.

• Institute of Oncology, Gliwice, Poland

autor

Rogolinski J.

autor

Lisowska K.

autor

Rzeszowska-Wolny J.

Bibliografia

• 1. Garrard, W. T. in: Nucleic Acids and Molecular Biology, Springer-Verlag, Berlin, vol.4, 1990, 163-175.
• 2. Bodnar, J. W. and Bradley, M. K J. Theor. Biol. 183 (1996) 1-7.
• 3. Pienta, K. J., Partin, A. W. and Coffey, D. S. Cancer Res. 49 (1989) 2525-2532.
• 4. Mirkovitch, J., Mirault, M-E. and Laemmli, U. K. Cell 39 (1984) 223-232.
• 5. Thompson, E. M., Christians, E., Stinnakre, M-G. and Renard, J-P. Mol. Cell. Biol. 14 (1994) 4694-4703.
• 6. Lisowska, K., Krawczyk, Z., Widłak, W., Wolniczek, P. and Wiśniewski, J. Biochim. Biophys. Acta 1219 (1994) 64-72.
• 7. Sambrook, J., Fritsch, E. F. and Maniatis, T. Molecular cloning, a laboratory manual. Cold Spring Harbor Laboratory Press, New York, 1989.
• 8. Cockerill, P. N. and Garrard, W. T. Cell 44 (1986) 273-282.
• 9. Widłak, P., Rogoliński, J. and Rzeszowska-Wolny, J. Acta Biochim. Polon. 42 (1995) 205-210.
• 10. Boulikas, T. J. Cell. Biochem. 52 (1993) 14-22.
• 11. Lisowska, K., Loch, T., Fiszer-Kierzkowska, A., Ścieglińska, D. and Krawczyk, Z. Acta Biochim. Polon. 44 (1997) 147-152.
• 12. Kellum, R. and Schedl, P. Cell 64 (1991) 941-950.
• 13. Krawczyk, Z., Wiśniewski, J., Mackiewicz, M., Biesiada, E. and Chorąży M. Biochim. Biophys. Acta 1009 (1989) 237-243.
• 14. Zakeri, Z. F., Welch, W. J. and Wolgemuth, D. J. J. Cell Biol. 111 (1990) 1785-1792.