Journal of Cell Science, Vol 106, Issue 1 431-439, Copyright © 1993 by Company of Biologists

JOURNAL ARTICLES

Immunological characterization of lamins in the nuclear matrix of onion cells

A Minguez and S Moreno Diaz de la Espina
Laboratorio de Biologia Celular y Molecular Vegetal, Centro de Investigaciones Biologicas, Madrid, Spain.

We have used polyclonal and monoclonal antibodies against different lamins from vertebrates, and the IFA antibody recognizing all kinds of intermediate filament proteins, to investigate the lamins of the nuclear matrix of Allium cepa meristematic root cells. All the antibodies react in the onion nuclear matrix with bands in the range of 60-65 kDa, which are enriched in the nuclear matrix after urea extraction, and do not crossreact with other antibodies recognizing intermediate filaments in plants (AFB, anti-vimentin and MAC 322), ruling out crossreaction with contaminating intermediate filaments of cytoplasmic bundles. In 2-D blots the chicken anti-lamin serum reacts with one spot at 65 kDa and pI 6.8 and the anti B-type lamin antibodies with another one at 64 kDa and pI 5.75. Both crossreact with IFA. The lamin is localized at the nuclear periphery and the lamina by indirect immunofluorescence. Immunogold labelling of nuclear matrix sections reveals that the protein is not only associated with the lamina, but also with the internal matrix. Taken together these results reveal that higher plants, which do not possess an organized network of cytoplasmic intermediate filaments, nevertheless present a well-organized lamina containing lamins in which at least one of them is immunologically related to vertebrate lamin B. Our data confirm that lamins are very old members of the intermediate filament proteins that have been better conserved in plants during evolution than their cytoplasmic counterparts.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				I. Meier Composition of the plant nuclear envelope: theme and variations J. Exp. Bot., January 1, 2007; 58(1): 27 - 34. [Abstract] [Full Text] [PDF]

				X. Yang, L. Timofejeva, H. Ma, and C. A. Makaroff The Arabidopsis SKP1 homolog ASK1 controls meiotic chromosome remodeling and release of chromatin from the nuclear membrane and nucleolus J. Cell Sci., September 15, 2006; 119(18): 3754 - 3763. [Abstract] [Full Text] [PDF]

				R. Samaniego, S. Y. Jeong, C. de la Torre, I. Meier, and S. M. Diaz de la Espina CK2 phosphorylation weakens 90 kDa MFP1 association to the nuclear matrix in Allium cepa J. Exp. Bot., January 1, 2006; 57(1): 113 - 124. [Abstract] [Full Text] [PDF]

				T. CAVALIER-SMITH Economy, Speed and Size Matter: Evolutionary Forces Driving Nuclear Genome Miniaturization and Expansion Ann. Bot., January 1, 2005; 95(1): 147 - 175. [Abstract] [Full Text] [PDF]

				A. Rose, S. Manikantan, S. J. Schraegle, M. A. Maloy, E. A. Stahlberg, and I. Meier Genome-Wide Identification of Arabidopsis Coiled-Coil Proteins and Establishment of the ARABI-COIL Database Plant Physiology, March 1, 2004; 134(3): 927 - 939. [Abstract] [Full Text] [PDF]

				A. Rose, F. Gindullis, and I. Meier A novel alpha-helical protein, specific to and highly conserved in plants, is associated with the nuclear matrix fraction J. Exp. Bot., April 1, 2003; 54(385): 1133 - 1141. [Abstract] [Full Text] [PDF]

				S. L. Irons, D. E. Evans, and F. Brandizzi The first 238 amino acids of the human lamin B receptor are targeted to the nuclear envelope in plants J. Exp. Bot., March 1, 2003; 54(384): 943 - 950. [Abstract] [Full Text] [PDF]

				C. Dreuillet, J. Tillit, M. Kress, and M. Ernoult-Lange In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C Nucleic Acids Res., November 1, 2002; 30(21): 4634 - 4642. [Abstract] [Full Text] [PDF]

				C. R. Cowan, P. M. Carlton, and W. Z. Cande The Polar Arrangement of Telomeres in Interphase and Meiosis. Rabl Organization and the Bouquet Plant Physiology, February 1, 2001; 125(2): 532 - 538. [Full Text]

				I. Meier A Novel Link between Ran Signal Transduction and Nuclear Envelope Proteins in Plants Plant Physiology, December 1, 2000; 124(4): 1507 - 1510. [Full Text]

				G. Morisawa, A. Han-yama, I. Moda, A. Tamai, M. Iwabuchi, and T. Meshi AHM1, a Novel Type of Nuclear Matrix-Localized, MAR Binding Protein with a Single AT Hook and a J Domain-Homologous Region PLANT CELL, October 1, 2000; 12(10): 1903 - 1916. [Abstract] [Full Text]

				P. A. Harder, R. A. Silverstein, and I. Meier Conservation of Matrix Attachment Region-Binding Filament-Like Protein 1 among Higher Plants Plant Physiology, January 1, 2000; 122(1): 225 - 234. [Abstract] [Full Text] [PDF]

				F. Gindullis, N. J. Peffer, and I. Meier MAF1, a Novel Plant Protein Interacting with Matrix Attachment Region Binding Protein MFP1, Is Located at the Nuclear Envelope PLANT CELL, September 1, 1999; 11(9): 1755 - 1768. [Abstract] [Full Text]

				F. Gindullis and I. Meier Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope PLANT CELL, June 1, 1999; 11(6): 1117 - 1128. [Abstract] [Full Text]

				P Hozak, A. Sasseville, Y Raymond, and P. Cook Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells J. Cell Sci., January 2, 1995; 108(2): 635 - 644. [Abstract] [PDF]

				A Minguez, S Franca, and S Moreno Diaz de la Espina Dinoflagellates have a eukaryotic nuclear matrix with lamin-like proteins and topoisomerase II J. Cell Sci., January 10, 1994; 107(10): 2861 - 2873. [Abstract] [PDF]