Binding of matrix attachment regions to lamin B1

Ludérus, M.E.E.; Graaf, A. De; Mattia, Elena Di; Blaauwen, Jan L. den; Grande, M.A.; Jong, Luitzen de; Driel, Roel van

doi:10.1016/0092-8674(92)90245-8

Cited by 308 publications

(213 citation statements)

References 58 publications

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“…The nuclear lamins are a group of intermediate filament proteins that constitute the nuclear lamina, which is a filamentous protein network that lines the inner membrane of the animal nuclear envelope (McKeon et al, 1986). It has been shown that rat lamin A and lamin B have MAR binding activity (Luderus et al, 1992(Luderus et al, , 1994 and that the polymerized state of the lamins is necessary for their DNA binding specificity (Zhao et al, 1996). These findings suggest a role for the nuclear lamins in attaching chromatin to the nuclear envelope.…”

Section: Introductionmentioning

confidence: 90%

Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope

Gindullis

Meier

1999

Plant Cell

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Recently, it has been suggested that nuclear processes, such as replication, transcription, and splicing, are spatially organized and associated with a nuclear framework called the nuclear matrix, a structure of unknown molecular composition. It has been shown that chromatin is attached to the nuclear matrix via specific DNA fragments called matrix attachment regions (MARs). We have begun to dissect the plant nuclear matrix by isolating a DNA binding protein with specific affinity for MARs. Here, it is shown that MAR binding filament-like protein 1 (MFP1) is associated with specklelike structures at the nuclear periphery that are part of isolated nuclei and the nuclear matrix. A predicted N-terminal transmembrane domain is necessary for the specific targeting of MFP1 to the speckles, indicating an association with the nuclear envelope-endoplasmic reticulum continuum. In addition, it is shown that a marker protein for plant microtubule organizing centers, which has been shown to be localized on the outside of the plant nuclear envelope, is also part of the nuclear matrix. These findings indicate a close and previously undescribed connection in plants between the nuclear envelope and the internal nuclear matrix, and they suggest a function for MFP1 in attaching chromatin to specific sites at the nuclear periphery. INTRODUCTIONThe nuclear matrix hypothesis proposes a structural framework for the eukaryotic nucleus that is similar to the cytoskeleton. Biochemically, the nuclear matrix is defined as the insoluble material that remains after extraction of nuclei with high-salt solutions (Berezney and Coffey, 1974) or with the chaotropic agent lithium diiodosalicylate (Mirkovitch et al., 1984) and treatment with DNases. Electron microscopy has shown a network of fibers of ‫ف‬ 10 nm in diameter. These fibers resemble the intermediate filaments of the cytoskeleton. Because they can be detected only under certain preparation conditions (He et al., 1990), their in vivo existence has been somewhat controversial.The isolated nuclear matrix binds specifically to certain DNA elements called matrix attachment regions (MARs). MARs are generally AT-rich DNA sequences that are several hundred base pairs long and are localized in the noncoding regions of the DNA, often flanking genes (Gasser and Laemmli, 1987). MARs have a positive effect on gene expression (Allen et al., 1993(Allen et al., , 1996Mlynárová et al., 1996) that is believed to be due to the establishment of independent and transcriptionally active chromatin domains between two MARs (Spiker and Thompson, 1996). Although the nuclear matrix was identified more than 20 years ago (Berezney and Coffey, 1974), none of its structural components has been isolated and molecularly characterized from any organism. One strategy to identify such components has been to isolate proteins that specifically bind to MARs. A small number of MAR binding proteins have been purified and cloned from animals, and they subsequently have been shown to be localized in the nuclear matrix (von Kri...

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Section: Introductionmentioning

confidence: 90%

Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope

Gindullis

Meier

1999

Plant Cell

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“…Matrix attachment regions (MARS), containing extensive runs of AT residues, have been shown to confer position and orientation independence to transcriptional properties of several genes in vitro and in vivo [Stief et al, 1989;Phi-Van and Stratling, 1990;Gasser et al, 1989;von Kries et al, 1991;Luderus et al, 1992;Klehr et al, 1991;Bonifer et al, 19901. These stable gene attachment sites mediate long-range influences covering several hundred kb [Jarman and Higgs, 19881.…”

Section: Introductionmentioning

confidence: 99%

Nuclear architecture supports integration of physiological regulatory signals for transcription of cell growth and tissue‐specific genes during osteoblast differentiation

Stein

Wijnen

Lian

et al. 1994

J of Cellular Biochemistry

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During the past several years it has become increasingly evident that the three-dimensional organization of the nucleus plays a critical role in transcriptional control. The principal theme of this prospect will be the contribution of nuclear structure to the regulation of gene expression as functionally related to development and maintenance of the osteoblast phenotype during establishment of bone tissue-like organization. The contributions of nuclear structure as it regulates and i s regulated by the progressive developmental expression of cell growth and bone cell related genes will be examined. We will consider signalling mechanisms that integrate the complex and interdependent responsiveness to physiological mediators of osteoblast proliferation and differentiation. The focus will be on the involvement of the nuclear matrix, chromatin structure, and nucleosome organization in transcriptional control of cell growth and bone cell related genes. Findings are presented which are consistent with involvement of nuclear structure in gene regulatory mechanisms which support osteoblast differentiation by addressing four principal questions: 1 ) Does the representation of nuclear matrix proteins reflect the developmental stage-specific requirements for modifications in transcription during osteoblast differentiation? 2 ) Are developmental stage-specific transcription factors components of nuclear matrix proteins? 3) Can the nuclear matrix facilitate interrelationships between physiological regulatory signals that control transcription and the integration of activities of multiple promoter regulatory elements? 4) Are alterations in gene expression and cell phenotypic properties in transformed osteoblasts and osteosarcoma cells reflected by modifications in nuclear matrix proteins? There is a striking representation of nuclear matrix proteins unique to cells, tissues as well as developmental stages of differentiation, and tissue organization. Together with selective association of regulatory molecules with the nuclear matrix in a growth and differentiation-specific manner, there is a potential for application of nuclear matrix proteins in tumor diagnosis, assessment of tumor progression, and prognosis of therapies where properties of the transformed state of cells is modified. It i s realistic to consider the utilization of nuclear matrix proteins for targeting regions of cell nuclei and specific genomic domains on the basis of developmental phenotypic properties or tissue pathology. z 1994 WlIey-Llss, Inc

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“…Lamins are thought to play a role in the structural and functional organization of the cell nucleus. The nuclear lamina may provide mechanical stability and, in addition, it may help to organize chromatin [5][6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Identification of a conserved phosphorylation site modulating nuclear lamin polymerization

Stuurman

1997

FEBS Letters

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Mitotic lamin disassembly results from phosphorylation at specific sites. In vitro, lamins can form head-to-tail polymers that disassemble upon phosphorylation by cdc2 kinase. A co-immunoprecipitation assay, employing Drosophila nuclear lamin Dm 0 fragments was used to study the effect of phosphorylation on head-to-tail binding. Phosphorylation of serine-50 by cAMP-dependent kinase inhibited head-to-tail binding in the same manner as phosphorylation of serine-42 by cdc2 kinase. Results suggest that multiple pathways may be employed to disassemble nuclear lamins in vivo.

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Binding of matrix attachment regions to lamin B1

Cited by 308 publications

References 58 publications

Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope

Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope

Nuclear architecture supports integration of physiological regulatory signals for transcription of cell growth and tissue‐specific genes during osteoblast differentiation

Identification of a conserved phosphorylation site modulating nuclear lamin polymerization

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