Matrix attachment region binding protein MFP1 is localized in discrete domains at the nuclear envelope

Plant Cell

Volumn 11, Issue 6, 1999, Pages 1117-1128

  Gindullis, Frank ^a,b   Meier, Iris ^a  

^a DUPONT COMPANY   (United States)

^b UNIVERSITY OF KIEL   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

NICOTIANA TABACUM;

EID: 0033150016     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.11.6.1117     Document Type: Article

References (58)

1. Allen, G.C., Hall, G.E., Jr., Childs, L.C., Weissinger, A.K., Spiker, S., and Thompson, W.F. (1993). Scaffold attachment regions increase reporter gene expression in stably transformed plant cells. Plant Cell 5, 603-613.
2. Allen, G.C., Hall, G., Jr., Michalowski, S., Newman, W., Spiker, S., Weissinger, A.K., and Thompson, W.F. (1996). High-level transgene expression in plant cells: Effects of a strong scaffold attachment region from tobacco. Plant Cell 8, 899-913.
3. Berezney, R., and Coffey, D.S. (1974). Identification of a nuclear protein matrix. Biochem. Biophys. Res. Commun. 60, 1410-1470.
4. Beven, A., Guan, Y., Pear, J., Cooper, C., and Shaw, P. (1991). Monoclonal antibodies to plant nuclear matrix reveal intermediate filament-related components within the nucleus. J. Mol. Biol. 228, 41-57.
5. Boevink, P., Oparka, K., Santa Cruz, S., Martin, B., Betteridge, A., and Hawes, C. (1998). Stacks on tracks: The plant Golgi apparatus traffics on an actin/ER network. Plant J. 15, 441-447.
6. Bretscher, M.S., and Munro, S. (1993). Cholesterol and the Golgi apparatus. Science 261, 1280-1281.
7. Chevrier, V., Komesli, S., Schmitt, A.C., Vantard, M., Lambert, A.M., and Job, D. (1992). A monoclonal antibody, raised against mammalian centrosomes and screened by recognition of plant microtubule organizing centers, identifies a pericentriolar component in different cell types. J. Cell Sci. 101, 823-835.
8. Compton, D.A., and Cleveland, D.W. (1993). NuMA is required for proper completion of mitosis. J. Cell Biol. 120, 947-957.
9. Davis, L.I. (1995). The nuclear pore complex. Annu. Rev. Biochem. 64, 865-896.
10. Davis, S.J., and Vierstra, R.D. (1998). Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants. Plant Mol. Biol. 36, 521-528.
11. Dickinson, L.A., Joh, T., Kohwi, Y., and Kohwi-Shigematsu, T. (1992). A tissue-specific MAR/SAR DNA-binding protein with unusual binding site recognition. Cell 70, 631-645.
12. Ellenberg, J., Siggia, E.D., Moreira, J.E., Smith, C.L., Presley, J.F., Worman, H.J., and Lippincott-Schwartz, J. (1997). Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol. 138, 1193-1206.
13. Furukawa, K., Pante, N., Aebi, K., and Gerace, L. (1995). Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope. EMBO J. 14, 1626-1636.
14. Galili, G., Sengupta-Gopalan, C., and Ceriotti, A. (1998). The endoplasmic reticulum of plant cells and its role in protein maturation and biogenesis of oil bodies. Plant Mol. Biol. 38, 1-29.
15. Gasser, S.M., and Laemmli, U.K. (1987). A glimpse at chromosomal order. Trends Genet. 3, 16-22.
16. Göhring, F., Schwab, B.L., Nicotera, P., Leist, M., and Fackelmayer, F.O. (1997). The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target for apoptotic nuclear breakdown. EMBO J. 16, 7361-7371.
17. Görlich, D., and Mattaj, I.W. (1996). Nucleocytoplasmic transport. Science 271, 1513-1518.
18. Grebenok, R.J., Pierson, E., Lambert, G.M., Gong, F.-C., Afonso, C.L., Haldeman-Cahill, R., Carrington, J.C., and Galbraith, D.W. (1997a). Green-fluorescent protein fusions for efficient characterization of nuclear targeting. Plant J. 11, 573-586.
19. Grebenok, R.J., Lambert, G.M., and Galbraith, D.W. (1997b). Characterization of the targeted nuclear accumulation of GFP within the cells of transgenic plants. Plant J. 12, 685-696.
20. Hall, G., Jr., Allen, G.C., Loer, D.S., Thompson, W.F., and Spiker, S. (1991). Nuclear scaffolds and scaffold-attachment regions in higher plants. Proc. Natl. Acad. Sci. USA 88, 9320-9324.
21. Haseloff, J., Siemering, K.R., Prasher, D.C., and Hodge, S. (1997). Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly. Proc. Natl. Acad. Sci. USA 94, 2122-2127.
22. He, D., Nickerson, J.A., and Penman, S. (1990). Core filaments of the nuclear matrix. J. Cell Biol. 110, 569-580.
23. Heese-Peck, A., and Raikhel, N.V. (1998). The nuclear pore complex. Plant Mol. Biol. 38, 145-162.
24. Hicks, G.R., Smith, H.M.S., Lobreaux, S., and Raikhel, N.V. (1996). Nuclear import in permeabilized protoplasts from higher plants has unique features. Plant Cell 8, 1337-1352.
25. Knebel, W., Quader, H., and Schnepf, E. (1990). Mobile and immobile endoplasmic reticulum in onion bulb epidermis cells: Short- and long-term observations with a confocal laser scanning microscope. Eur. J. Cell Biol. 52, 328-340.
26. 1. Cell 70, 949-959.
27. Luderus, M.E.E., den Blaauwen, J.L., de Smit, O.J.B., Compton, D.A., and van Driel, R. (1994). Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove. Mol. Cell. Biol. 14, 6297-6305.
28. Lydersen, B.K., and Pettijohn, D.E. (1980). Human-specific nuclear protein that associates with the polar region of the mitotic apparatus: Distribution in a human/hamster hybrid cell. Cell 22, 489-499.
29. McKeon, F.D., Kirschner, M.W., and Caput, D. (1986). Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319, 463-468.
30. McNulty, A.K., and Saunders, M.J. (1992). Purification and immunological detection of pea nuclear intermediate filaments: Evidence for plant nuclear lamins. J. Cell Sci. 103, 407-414.
31. Meier, I., Phelan, T., Gruissem, W., Spiker, S., and Schneider, D. (1996). MFP1, a novel plant filament-like protein with affinity for matrix attachment region DNA. Plant Cell 8, 2105-2115.
32. Mewes, H.W., Hani, J., Pfeiffer, F., and Frishman, D. (1998). MIPS: A database for protein sequences and complete genomes. Nucleic Acids Res. 26, 33-37.
33. Minguez, A., and Moreno Diaz de la Espina, S. (1993). Immunological characterization of lamins in the nuclear matrix of onion cells. J. Cell Sci. 106, 431-439.
34. Mirkovitch, J., Mirault, M.-E., and Laemmli, U.K. (1984). Organization of the higher-order chromatin loop: Specific DNA attachment sites on nuclear scaffolds. Cell 39, 223-232.
35. Mlynárová, Ľ, Keizer, L.C.P., Stiekema, W.J., and Nap, J.-P. (1996). Approaching the lower limits of transgene variability. Plant Cell 8, 1589-1599.
36. Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G. (1997). Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6.
37. Pedrazzini, E., Villa, A., and Borgese, N. (1996). A mutant cytochrome b5 with a lengthened membrane anchor escapes from the endoplasmic reticulum and reaches the plasma membrane. Proc. Natl. Acad. Sci. USA 93, 4207-4212.
38. Renz, A., and Fackelmayer, F.O. (1996). Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA. Nucleic Acids Res. 24, 843-849.
39. Restrepo-Hartwig, M.A., and Ahlquist, P. (1996). Brome mosaic virus helicase- and polymerase-like proteins colocalize on the endoplasmatic reticulum at sites of viral RNA synthesis. J. Virol. 70, 8908-8916.
40. Sambrook, J., Fritsch, E.M., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
41. Schaad, M.C., Jensen, P.E., and Carrington, J.C. (1997). Formation of plant RNA virus replication complexes on membranes: Role of an endoplasmic reticulum-targeted viral protein. EMBO J. 16, 4049-4059.
42. Schafer, W.R., and Rine, J. (1992). Protein prenylation: Genes, enzymes, targets and functions. Annu. Rev. Genet. 30, 209-237.
43. Schmit, A.C., Stoppin, V., Chevrier, V., Job, D., and Lambert, A.M. (1994). Cell cycle dependent distribution of a centrosomal antigen at the perinuclear MTOC or at the kinetochores of higher plant cells. Chromosome 103, 343-351.
44. Spiker, S., and Thompson, W.F. (1996). Nuclear matrix attachment regions and transgene expression in plants. Plant Physiol. 110, 15-21.
45. Staehelin, L.A. (1997). The plant ER: A dynamic organelle composed of a large number of discrete functional domains. Plant J. 11, 1151-1165.
46. Stoppin, V., Vantard, M., Schmit, A.-C., and Lambert, A.M. (1994) Isolated plant nuclei nucleate microtubule assembly: The nuclear surface in higher plants has centrosome-like activity. Plant Cell 6, 1099-1106.
47. Stoppin, V., Lambert, A.M., and Vantard, M. (1996). Plant microtubule-associated proteins (MAPs) affect microtubule nucleation and growth at plant nuclei and mammalian centrosomes. Eur. J. Cell Biol. 69, 11-23.
48. Sukegawa, J., and Blobel, G. (1993). A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm. Cell 72, 29-38.
49. Verheijnen, R., Van Venrooij, W., and Ramaekers, F. (1988). The nuclear matrix: Structure and composition. J. Cell Sci. 90, 11-36.
50. von Arnim, A., Deng, X.W., and Stacey, M.G. (1998). Cloning vectors for the expression of green fluorescent protein fusion proteins in transgenic plants. Gene 221, 35-43.
51. von Heijne, G. (1992). Membrane protein structure prediction. Hydrophobicity analysis and positive-inside rule. J. Mol. Biol. 225, 487-494.
52. von Kries, J.P., Buhrmeister, H., and Strätling, W.H. (1991). A matrix/scaffold attachment region binding protein: Identification, purification and mode of binding. Cell 64, 123-135.
53. Watson, J.C., and Thompson, W.F. (1986). Purification and restriction endonuclease analysis of plant nuclear DNA. Methods Enzymol. 118, 57-75.
54. Wei, X., Samarabandu, J., Devdhar, R.S., Siegel, A.J., Acharya, R., and Berezney, R. (1998). Segregation of transcription and replication sites into higher order domains. Science 281, 1502-1505.
55. Whitmarsh, A.J., Cavanagh, J., Tournier, C., Yasuda, J., and Davis, R.J. (1998). A mammalian scaffold complex that selectively mediates MAP kinase activation. Science 281, 1671-1674.
56. Yang, C.H., and Snyder, M. (1992). The nuclear-mitotic apparatus protein (NuMA) is important in the establishment and maintenance of the bipolar mitotic spindle apparatus. Mol. Biol. Cell. 3, 1259-1267.
57. Yang, M., Ellenberg, J., Bonifacino, J.S., and Weissman, A.M. (1997). The transmembrane domain of a carboxyl-terminal anchored protein determines localization to the endoplasmic reticulum. J. Biol. Chem. 272, 1970-1975.
58. Zhao, K., Harel, A., Stuurman, N., Guedalia, D., and Gruenbaum, Y. (1996). Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state. FEBS Lett. 12, 161-164.