Modulation of plant nuclear matrix nucleolytic activity and specificity may result from interaction of nuclease-protein 14-3-3 complex with inner nuclear membrane lipids

• Autorzy: Lubocka J. , Kozubek A.
• Języki publikacji: EN

Abstrakty

EN

Plant cell nuclear matrix depleted in lipids exhibited approximately 50% lower endonucleolytic activity attributed to 32 kDa nuclease. Supplementation of delipidated matrix with phospholipids, sterols and glycolipids resulted in the recovery of nuclease activity. The extent of recovery is dependent upon the type of lipid used for reconstitution. The most effective (over 97%) in recovery of the nucleolytic activity were PC, PE, DGDG and stigmasterol. Some recovery is also observed when other natural amphiphilic molecules are studied (resorcinolic lipids). Recombinant plant protein 14-3-3 showed ability for direct interaction with lipid monolayers. The interaction was confirmed by analysis of the monolayer collected from the subphase after incubation with protein 14-3-3. Deletion of the 12 kDa N-terminal fragment of the protein 14-3-3 abolished its ability for binding to lipid monolayer. The results suggest that in vivo direct interaction of protein 14-3-3 with nuclear envelope lipids may participate in modulation of the nuclease 32 kDa activity. A postulated model of the interactions is discussed.

Słowa kluczowe

EN

nuclease activity; cell; lipid; interaction; galactolipid; sterol; nuclease-protein interaction; nuclear matrix; membrane lipid; phospholipid; plant

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 1998
• Tom: 03
• Numer: 1
• Opis fizyczny: p.57-73,fig.

Twórcy

autor

Lubocka J.

• University of Wroclaw, Przybyszewskiego 63-77, 51-148 Wroclaw, Poland

autor

Kozubek A.

Bibliografia

• 1. Berezney, R. and Coffey, D. S. J. Cell Biol. 73 (1977) 616-637
• 2. Wunderlich, F. J. Cell Biol. 73 (1977) 271-287
• 3. Schweiger, A. and Kostka, G. Biochem. Biophys. Res. Commum. 114 (1983) 1-12
• 4. van der Velden, H. M. and Wanka, F. Mol. Biol. Rep. 12 (1987) 69-77
• 5. Verhereijen, R., van Vemooij, W. and Ramaekers, F. J. Cell Sci. 90 (1988) 11-36
• 6. Jaberoboansari, A., Landis, M. R. and Wallen, C. A. Radiation Res. 119 (1989) 57-72
• 7. Warters, R. L. Radiation Res. 115 (1988) 258-272
• 8. Kaufman, S. H., Fields, M. R. and Sharper, J. H. Meth. Achiev. Exp. Pathol. 12 (1986) 141-171
• 9. Łubocka, J., Szopa, J. and Kozubek, A. Acta Biochim. Polon. 42 (1995) 211-216
• 10. Schmit, H. S., Puvion, E., Buchholtz, L. A. and Berezney, R., J. Cell Biol. 99 (1984) 1794-1802
• 11. Jones, C. and Su, R. T. Nucleic Acid Res. 10 (1982) 5517-5532
• 12. Rudnicki, R., Rzepecki, R. and Szopa, J. J. Plant. Physiol. 132 (1988) 658-663
• 13. Rzepecki, R., Bułaj, G. and Szopa, J. J. Plant Physiol. 134 (1989) 354-369
• 14. Rzepecki, R., Szmidzinski, R., Bode, R. and Szopa, J. J. Plant Physiol. 139 (1992) 284-288
• 15. Markiewicz E., Wilczyński G., Rzepecki R., Kulma A. and Szopa J., Cell. Mol. Biol. Lett. 1 (1996) 391-415
• 16. Bihn, E. A., Paul, A., Wang, S.W., Erolos, G. W. and Ferl, R. J. Plant J. 12 (1997) 1439-1445
• 17. Szopa, J. Acta Bioch. Polon. 2 (1995) 183-190
• 18. Pepinski, R. B., Tizard, R., Matiano, R. L., Sinclair, J. K. and Wallner, B. P. J. Biol. Chem. 263 (1988) 10799-10811
• 19. Klee, C. B. Biochemistry 27 (1988) 6645-6653
• 20. Leffers, H., Madsen, P., Rassmusen, H. H. and Celis, J. E. J. Mol. Biol. 231 (1993) 982-988
• 21. Lubocka, J., Szopa, J. and Kozubek, A. Acta Biochim. Polon. 42 (1995) 217- 220
• 22. Luthe, D. S. and Quatrano, R. S. Plant Physiol. 65 (1980) 305-308
• 23. Slatter, R. E., Dupree, P. and Gray, J. Plant Cell 3 (1991) 1239-1250
• 24. Bradford, M. Anal. Biochem. 272 (1976) 248-254
• 25. Szopa, J., Bocher, M. and Wagner, K. G. J. Plant Physiol. 109 (1983) 291-300
• 26. Jones, H. A., Martin, H., Madrazo, J., Robinson, K. A., Roseboom, P. H., Patel, Y., Howell, S. A. and Aitken, A. J. Mol. Biol. 245 (1995) 375-384
• 27. Radin, N. S.(1981) Methods Enzymol. 72, 5-7
• 28. Towbin, H., Stachelin, T. and Gordon, J. Proc. Natl. Acad. Sci. USA 76 (1979) 4350-4354
• 29. van Horf, R., van Klompenburg, W., Pilon, M., Kozubek, A., de Korte-Kool, G., Demel, R. A., Weisbeek, P. J. and de Kruijff, B. J. Biol. Chem. 286 (1993) 4037-4042
• 30. Kozubek, A., Sikorski, A. F. and Szopa, J. in: Molecular organisation of cell II. Lipids, Liposomes and Biological Membranes. (Kozubek, A., Ed.) 2nd edition, Wroclaw University Press, Wroclaw, 1996, 20-21 ’
• 31. Higgins, J. A. in: Biological Membranes - a Practical Approach. (Findlay, J. B. C. and Evans W. H., Eds.) IRL Press, Oxford, Washington DC, 1987, 103-137
• 32. Roughan, P. G. and Batt, R. D. Anal. Biochem. 22 (1986) 74-88
• 33. Sikorski, A. F., Terlecki, G., Zagon, J. S. and Goodman, S. R. J. Cell. Biol. 114 (1991) 313-318
• 34. Roth D., Morgan A., Martin H., Jones D., Aitken A. and Burgoyne R. Biochem. J. 310 (1994) 305-310
• 35. Leffers, H., Madsen, P., Rasmussen, H. H., Honore, B., Anderson, A. H., Walbum, E., Vandekerckhove, J. and Celis, J. E. J. Mol. Biol. 231 (1993) 982-998
• 36. Lubocka, J. and Kozubek, A. Cell. Mol. Biol. Lett. 2 (1997) 233