Interphase nuclear envelope lamins form a discontinuous network that interacts with only a fraction of the chromatin in the nuclear periphery

Paddy, Michael R.; Belmont, Andrew S.; Saumweber, Harald; Agard, David A.; Sedat, John W.

doi:10.1016/0092-8674(90)90243-8

Cited by 188 publications

(102 citation statements)

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“…This idea is consistent with the finding that the nuclear membrane appeared to be essential for the initiation of DNA replication in G 1 cells (Dingwall and Laskey 1992;Leno et al 1992). Also, interactions between the nuclear envelope and a small fraction of the chromatin have been reported (Paddy et al 1990), which is in favor of the idea that centromeres are bound to the nuclear membrane. At the nuclear periphery, as such, the centromeres of chromosome 11 were randomly distributed relative to each other, as has also been found for centromeres of chromosome 1 by Van Dekken et al (1990).…”

Section: Discussionsupporting

confidence: 89%

The nuclear position of pericentromeric DNA of chromosome 11 appears to be random in GO and non-random in G1 human lymphocytes

et al. 1994

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The nuclear position of pericentromeric DNA of chromosome 11 appears to be random in G0 and non-random in G1 human lymphocytes Hulspas, R.; Houtsmuller, A.; Krijtenburg, P.-J.; Bauman, J.G.J.; Nanninga, N. Published in: Chromosoma DOI:10.1007/BF00352253 Link to publication Citation for published version (APA):Hulspas, R., Houtsmuller, A., Krijtenburg, P-J., Bauman, J. G. J., & Nanninga, N. (1994). The nuclear position of pericentromeric DNA of chromosome 11 appears to be random in G0 and non-random in G1 human lymphocytes. Chromosoma, 103, 286-292. DOI: 10.1007/BF00352253 General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 12 May 2018Chromosoma ( Abstract. The nuclear topography of pericentromeric DNA of chromosome 11 was analyzed in G O (nonstimulated) and G 1 [phytohemagglutinin (PHA) stimulated] human lymphocytes by confocal microscopy. In addition to the nuclear center, the centrosome was used as a second point of reference in the three-dimensional (3D) analysis. Pericentromeric DNA of chromosome 11 and the centrosome were labeled using a combination of fluorescent in situ hybridization (FISH) and immunofluorescence. To preserve the 3D morphology of the cells, these techniques were performed on whole cells in suspension. Three-dimensional images of the cells were analyzed with a recently developed 3D software program (Interactive Measurement of Axes and Positioning in 3 Dimensions). The distribution of the chromosome 11 centromeres appeared to be random during the G O stage but clearly non-random during the G 1 stage, when the nuclear center was used as a reference point. Further statistical analysis of the G1 cells revealed that the centromeres were randomly distributed in a shell underlying the nuclear membrane. A topographical relationship between the centrosome and the centromeres appeared to be absent during the G O and G I stages of the cell cycle.

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Section: Discussionsupporting

confidence: 89%

The nuclear position of pericentromeric DNA of chromosome 11 appears to be random in GO and non-random in G1 human lymphocytes

et al. 1994

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“…Additional confocal microscopy analysis revealed subregions of the nuclear envelope with a higher intensity staining (our unpublished results). Such subregions of intense staining are characteristic of lamin staining in other metazoans (Paddy et al, 1990) (Figure 2). The localization of Ce- were stained with affinity purified polyclonal antibodies to Ce-lamin (primary), and Cy3-conjugated antirabbit antibodies (secondary) (b,d,f,g).…”

Section: Lmn-1 Encodes a Single Type-b Lamin Proteinmentioning

confidence: 99%

“…Additional confocal microscopy analysis revealed subregions of the nuclear envelope with a higher intensity staining (our unpublished results). Such subregions of intense staining are characteristic of lamin staining in other metazoans (Paddy et al, 1990) (Figure 2). The localization of Ce- lamin to the nuclear periphery, its pattern in the nuclear periphery, and its sequence homology to other known type-B lamins, all suggest that lmn-1 is the unique type-B lamin ortholog in C. elegans.…”

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confidence: 99%

Essential Roles forCaenorhabditis elegansLamin Gene in Nuclear Organization, Cell Cycle Progression, and Spatial Organization of Nuclear Pore Complexes

Ben-Shahar

Riemer

et al. 2000

MBoC

379

360

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Caenorhabditis elegans has a single lamin gene, designated lmn-1 (previously termed CeLam-1). Antibodies raised against the lmn-1 product (Ce-lamin) detected a 64-kDa nuclear envelope protein. Ce-lamin was detected in the nuclear periphery of all cells except sperm and was found in the nuclear interior in embryonic cells and in a fraction of adult cells. Reductions in the amount of Ce-lamin protein produce embryonic lethality. Although the majority of affected embryos survive to produce several hundred nuclei, defects can be detected as early as the first nuclear divisions. Abnormalities include rapid changes in nuclear morphology during interphase, loss of chromosomes, unequal separation of chromosomes into daughter nuclei, abnormal condensation of chromatin, an increase in DNA content, and abnormal distribution of nuclear pore complexes (NPCs). Under conditions of incomplete RNA interference, a fraction of embryos escaped embryonic arrest and continue to develop through larval life. These animals exhibit additional phenotypes including sterility and defective segregation of chromosomes in germ cells. Our observations show that lmn-1 is an essential gene in C. elegans, and that the nuclear lamins are involved in chromatin organization, cell cycle progression, chromosome segregation, and correct spacing of NPCs. INTRODUCTIONThe nuclear lamina is a filamentous meshwork that is present between the inner nuclear membrane and the peripheral chromatin. The inner nuclear membrane and the nuclear lamina are involved in organizing nuclear structure and regulating nuclear events. These include the organization of the higher order structure of chromatin and regulation of nuclear assembly and disassembly. The nuclear lamina is a primary target for caspases in apoptosis (reviewed in Goldberg et al., 1999b). Lamins are the major proteins of the nuclear lamina. They are classified as type-V intermediate filaments and are composed of an ␣-helical rod domain flanked by a short amino (head) and a long carboxy (tail) domains. The rod domain of lamins is 52-nm long and contains four ␣-helices, each composed of heptad repeats. Coiled-coil interactions and head-to-tail associations between lamin monomers form 10-to 200-nm thick lamin filaments (reviewed in Stuurman et al., 1998) In vivo, lamin filaments are closely associated with the chromatin fibers (Belmont et al., 1993). In vitro, lamins can bind interphase chromatin (Hoger et al., 1991;Yuan et al., 1991;Taniura et al., 1995;Ulitzur et al., 1997;Goldberg et al., 1999a), mitotic chromosomes (Glass and Gerace, 1990;Glass et al., 1993), or specific DNA sequences (Shoeman and Traub, 1990;Luderus et al., 1992;Luderus et al., 1994;Baricheva et al., 1996;Zhao et al., 1996). The binding site of vertebrate lamins to chromatin is localized to specific sequences in the tail domain and can be displaced with the core histones H2A and H2B (Taniura et al., 1995;Goldberg et al., 1999a).The composition of the nuclear lamina varies in different cell types and is under developmental regulation ...

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“…In rare cases, such as in the nucleus of the oocyte of Xenopus laevis, the lamina appears as a dense fibrous network occasionally having a lattice-like appear-ance (Aebi et al, 1986). In other cell types the lamina network does not form regular arrays, but may be discontinuous and as such may cover at most half of the inner nuclear membrane (Paddy et al, 1990). However, this may not be true of all cell types (Belmont et al, 1993).…”

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confidence: 95%

Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication.

Moir

Montag-Lowy

Goldman

1994

The Journal of Cell Biology

247

202

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Abstract. The nuclear lamins form a fibrous structure, the nuclear lamina, at the periphery of the nucleus. Recent results suggest that lamins are also present as foci or spots in the nucleoplasm at various times during interphase of the cell cycle (Goldman, A. E., R. D. Moir, M. Montag-Lowy, M. Stewart, and R. D. Goldman. 1992. J. Cell Biol. 104:725-732; Bridger, J. M., I. R. Kill, M. O'Farrell, and C. J. Hutchison. 1993. J. Cell Sci. 104:297-306). In this report we demonstrate that during mid-late S-phase, nuclear foci detected with lamin B antibodies are coincident with sites of DNA replication as detected by the colocalization of sites of incorporation of bromodeoxyuridine (BrDU) or proliferating cell nuclear antigen (PCNA). The relationship between lamin B and BrDU is not maintained in the following G1 stage of the cell cycle. Furthermore, the nuclear staining patterns seen with antibodies directed against lamins A and C in mid-late S-phase do not coalign with the lamin B/BrDU-containing structures. These results imply that there is a role for lamin B in the organization of replicating chromatin during S phase.T He nuclear lamina is a thin fibrous structure that underlies the inner nuclear membrane (Gerace and Burke, 1988;Nigg, 1992;Moir and Goldman, 1993). The proteins of the lamina, the nuclear lamins, comprise the type V intermediate filament (IF) 1 proteins. The lamins share the common structural features of cytoskeletal IF proteins, including a highly conserved central alpha helical rod domain and two nonalpha-helical flanking domains (Steinert and Parry, 1985;Stewart, 1993). There may be up to five different nuclear lamin proteins in the lamina polymer, depending on cell type (Lehner et al., 1986; Kauffmann, 1989). These different lamins are classified into two groups: the A type which are found only in differentiated cells and the B type which are found in both undifferentiated and differentiated cell types. In mammalian cells there are two major A-type lamins (lamins A and C) produced by alternate splicing of the same gene. These lamins have identical sequences, except for a 90-amino acid extension at the COOH terminus of lamin A. The B type lamins are termed B1 and B2 (Nigg, 1992). The nature of the molecular interactions between the different lamins and the structure of the assembled polymer that results have not been clearly established (Stewart, 1993). In rare cases, such as in the nucleus of the oocyte of Xenopus laevis, the lamina appears as a dense fibrous network occasionally having a lattice-like appear-

show abstract

Interphase nuclear envelope lamins form a discontinuous network that interacts with only a fraction of the chromatin in the nuclear periphery

Cited by 188 publications

References 48 publications

The nuclear position of pericentromeric DNA of chromosome 11 appears to be random in GO and non-random in G1 human lymphocytes

The nuclear position of pericentromeric DNA of chromosome 11 appears to be random in GO and non-random in G1 human lymphocytes

Essential Roles forCaenorhabditis elegansLamin Gene in Nuclear Organization, Cell Cycle Progression, and Spatial Organization of Nuclear Pore Complexes

Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication.

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