Advertisement
Journal Articles
Purification and immunological detection of pea nuclear intermediate filaments: evidence for plant nuclear lamins
A.K. McNulty, M.J. Saunders
Journal of Cell Science 1992 103: 407-414;

A major structural component of the inner face of the nuclear envelope in vertebrates and invertebrates is the nuclear lamina, an array of 1–3 extrinsic membrane proteins, lamins A, B and C. These proteins are highly homologous to intermediate filaments and are classified as type V. We report the first purification, antigenic characterization and immunocytochemical localization of putative plant lamin proteins from pea nuclei. We conclude that plant cells contain this ancestral class of intermediate filaments in their nuclei and that regulation of nuclear envelope assembly/disassembly and mitosis in plants may be similar to that in animal cells.

REFERENCES

    1. Aebi U.,
    2. Cohn J.,
    3. Buhle. and
    4. Gerace L.
    (1986). The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323, 560–564
    OpenUrlCrossRefPubMed
    1. Beven A.,
    2. Guan Y.,
    3. Pert J.,
    4. Cooper C. and
    5. Shaw P.
    (1991). Monoclonal antibodies to plant nuclear matrix reveal intermediate filament-related components within the nucleus. J. Cell Sci 98, 293–302
    OpenUrlAbstract/FREE Full Text
    1. Dawson P. J.,
    2. Hulme J. S. and
    3. Lloyd C. W.
    (1985). Monoclonal antibody to intermediate filament antigen cross-reacts with higher plant cells. J. Cell Biol 100, 1793–1798
    OpenUrlAbstract/FREE Full Text
    1. Dessev G.,
    2. Iovcheva-Dessev C.,
    3. Bischoff J. R.,
    4. Beach D. and
    5. Goldman R.
    (1991). A complex containing p34cdc2 and cyclin B414phosphorylates the nuclear lamin and disassembles nuclei of clam oocytes in vitro. J. Cell Biol 112, 523–533
    OpenUrlAbstract/FREE Full Text
    1. Dwyer N. and
    2. Blobel G.
    (1976). A modified procedure for the isolation of a pore complex lamina fraction from rat liver nuclei. J. Cell Biol 70, 581–591
    OpenUrlAbstract/FREE Full Text
    1. Feiler H. S. and
    2. Jacobs T. W.
    (1990). Cell division in higher plants: A cdc2 gene, its 34-kDa product, and histone H1 kinase activity in pea. Proc. Natl Acad. Sci. U.S.A 87, 5397–5401
    OpenUrlAbstract/FREE Full Text
    1. Fisher D.,
    2. Chaudhary N. and
    3. Blobel G.
    (1986). cDNA sequencing of nuclear lamins A and C reveals primary and secondary homology to intermediate filament proteins. Proc. Natl Acad. Sci. U.S.A 83, 6450–6454
    OpenUrlAbstract/FREE Full Text
    1. Geisler N. and
    2. Weber K.
    (1982). The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. EMBO J 1, 1649–1656
    OpenUrlPubMedWeb of Science
    1. Gerace L.
    (1986). Nuclear lamina and organization of nuclear architecture. Trends Biochem. Sci 11, 443–446
    OpenUrlCrossRefWeb of Science
    1. Gerace L. and
    2. Blobel G.
    (1980). The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19, 277–287
    OpenUrlCrossRefPubMedWeb of Science
    1. Gerace L.,
    2. Comeau C. and
    3. Benson M.
    (1984). Organization and modulation of nuclear lamina structure. J. Cell Sci.Suppl 1, 137–160
    OpenUrlPubMed
    1. Glass J. R. and
    2. Gerace L.
    (1990). Lamins A + C bind and assemble at the surface of mitotic chromosomes. J. Cell Biol 111, 1047–1057
    OpenUrlAbstract/FREE Full Text
    1. Goodbody K. C.,
    2. Hargreaves A. J. and
    3. Lloyd C. W.
    (1989). On the distribution of microtubule-associated intermediate filament antigens in plant cells. J. Cell Sci 93, 427–438
    OpenUrlAbstract/FREE Full Text
    1. Hargreaves A. L.,
    2. Dawson P. J.,
    3. Butcher G. W.,
    4. Larkins A.,
    5. Goodbody K. C. and
    6. Lloyd C. W.
    (1989). A monoclonal antibody raised against cytoplasmic fibrillar bundles from carrot cells, and its cross-reaction with animal intermediate filaments. J. Cell Sci 92, 371–378
    OpenUrlAbstract/FREE Full Text
    1. Harper J. D. I.,
    2. Rao P. N. and
    3. John P. C.
    (1990). The mitosis-specific monoclonal antibody MPM-2 recognizes phosphoproteins associated with the nuclear envelope in Chlamydomonas reinhardtii cells. Eur. J. Cell Biol 51, 272–278
    OpenUrlPubMed
    1. John P. C. L.,
    2. Sek F. J. and
    3. Lee M. G.
    (1989). A homologue of the cell division cycle control protein p34cdc2 participates in the cell division cycle of Chlamydomonas and a similar protein is detectable in higher plants and remote taxa. Plant Cell 1, 1185–1193
    OpenUrlAbstract/FREE Full Text
    1. Krohne G. and
    2. Benavente R.
    (1986). The nuclear lamins: Multigene family of proteins in evolution and differentiation. Exp. Cell Res 162, 1–10
    OpenUrlCrossRefPubMedWeb of Science
    1. Laemmli U. K.
    (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685
    OpenUrlCrossRefPubMed
    1. Lehner C. F.,
    2. Kurer V.,
    3. Eppenberger H. M. and
    4. Nigg E. A.
    (1986). The nuclear lamin protein family in higher vertebrates. J. Biol. Chem 261, 13293–13301
    OpenUrlAbstract/FREE Full Text
    1. Markwell M. A. K.,
    2. Haas S. M.,
    3. Bieber L. L. and
    4. Tolbert N. E.
    (1978). A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem 87, 206–210
    OpenUrlCrossRefPubMedWeb of Science
    1. McKeon F. D.,
    2. Kirschner M. W. and
    3. Kaput D.
    (1986). Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319, 463–468
    OpenUrlCrossRefPubMed
    1. Osborn M. and
    2. Weber K.
    (1986). Intermediate filament proteins: a multigene family distinguishing major cell lineages. Trends Biochem. Sci 11, 469–472
    OpenUrlCrossRef
    1. Osman M.,
    2. Paz M.,
    3. Landesman Y.,
    4. Fainsod A. and
    5. Gruenbaum Y.
    (1990). Molecular analysis of the Drosophila nuclear lamin gene. Genomics 8, 217–224
    OpenUrlCrossRefPubMed
    1. Ottaviano Y. and
    2. Gerace L.
    (1986). Phosphorylation of the nuclear lamins during interphase and mitosis. J. Biol. Chem 260, 624–632
    OpenUrl
    1. Parke J. M.,
    2. Miller C. C. J.,
    3. Cowell I.,
    4. Dodson A.,
    5. Dowding A.,
    6. Downes M.,
    7. Duckett J. G. and
    8. Anderton B. J.
    (1987). Monoclonal antibodies against plant proteins recognize animal intermediate filaments. Cell Motil. Cytoskel 8, 312–323
    OpenUrlCrossRefPubMed
    1. Peter M.,
    2. Nakagawa J.,
    3. Doree M.,
    4. Labbe J. C. and
    5. Nigg E. A.
    (1990). In vitro disassembly of the nuclear lamina and M-phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61, 591–602
    OpenUrlCrossRefPubMedWeb of Science
    1. Pruss R. M.,
    2. Mirsky R.,
    3. Raff M. C.,
    4. Thorpe R.,
    5. Dowding A. J. and
    6. Anderton B. H.
    (1981). All classes of intermediate filaments share a common antigenic determinant defined by a monoclonal antibody. Cell 27, 419–428
    OpenUrlCrossRefPubMedWeb of Science
    1. Ross J. H.,
    2. Hutchings A.,
    3. Butcher G. W.,
    4. Lane E. B. and
    5. Lloyd C. W.
    (1991). The intermediate filament-related system of higher plant cells shares an epitope with cytokeratin 8. J. Cell Sci 99, 91–88
    OpenUrlAbstract/FREE Full Text
    1. Chopra R. N. and
    2. Bhathla S. C.
    1. Saunders M. J.
    (1990). Calcium and cytokinin in mosses. Bryophytes: Physiology and Biochemistry, (ed. Chopra R. N. and Bhathla S. C.)., pp. 103–118 Crit. Rev. Sci.
    1. Steinert P. M.,
    2. Steven A. C. and
    3. Roop D. R.
    (1985). The molecular biology of intermediate filaments. Cell 42, 411–419
    OpenUrlCrossRefPubMedWeb of Science
    1. Traub P.,
    2. Scherbarth A.,
    3. Willingale-Theune J. and
    4. Traub U.
    (1988). Large scale co-isolation of vimentin and nuclear lamins from Ehrlich ascites tumor cells cultured in vitro. Prep. Biochem 18, 381–404
    OpenUrlPubMed
    1. Ward G. E. and
    2. Kirshner M. W.
    (1990). Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C. Cell 61, 561–577
    OpenUrlCrossRefPubMedWeb of Science
Back to top

 Download PDF

Email
Journal Articles
Purification and immunological detection of pea nuclear intermediate filaments: evidence for plant nuclear lamins
A.K. McNulty, M.J. Saunders
Journal of Cell Science 1992 103: 407-414;
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
Citation Tools
Alerts

Article navigation

Other journals from The Company of Biologists

Advertisement

2020 at The Company of Biologists

Despite the challenges of 2020, we were able to bring a number of long-term projects and new ventures to fruition. While we look forward to a new year, join us as we reflect on the triumphs of the last 12 months.

Mole – The Corona Files

"This is not going to go away, 'like a miracle.' We have to do magic. And I know we can."

Mole continues to offer his wise words to researchers on how to manage during the COVID-19 pandemic.

Cell scientist to watch – Christine Faulkner

In an interview, Christine Faulkner talks about where her interest in plant science began, how she found the transition between Australia and the UK, and shares her thoughts on virtual conferences.

Read & Publish participation extends worldwide

“The clear advantages are rapid and efficient exposure and easy access to my article around the world. I believe it is great to have this publishing option in fast-growing fields in biomedical research.”

Dr Jaceques Behmoaras (Imperial College London) shares his experience of publishing Open Access as part of our growing Read & Publish initiative. We now have over 60 institutions in 12 countries taking part – find out more and view our full list of participating institutions.

JCS and COVID-19

For more information on measures Journal of Cell Science is taking to support the community during the COVID-19 pandemic, please see here.

If you have any questions or concerns, please do not hestiate to contact the Editorial Office.