Studies on Scaffold Attachment Sites and Their Relation to Genome Function

Gasser, Susan M.; Amati, Bruno; Cárdenas, María E.; Hofmann, Johannes

doi:10.1016/s0074-7696(08)60649-x

Cited by 194 publications

(113 citation statements)

References 167 publications

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“…These data indicate that a chromosome-internal array of -130 TTAGGG repeats does not become attached to the nuclear matrix. Since many previously described matrix attachment regions are much shorter than 800 bp (Gasser et al, 1989), this result is probably due to a functional difference between chromosome-internal and telomeric TTAGGG repeats rather than an effect of the length of the TTAGGG repeat array.…”

Section: Introductionmentioning

confidence: 85%

Human telomeres are attached to the nuclear matrix.

1992

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This report shows that human telomeres are tightly associated with the nuclear matrix. Telomere attachment is observed in several cell types and in all stages of interphase. Mapping experiments show that telomeres are anchored via their TTAGGG repeats; a subtelomeric repeat located immediately proximal to the telomeric TTAGGG repeats is quantitatively released from the nuclear matrix by restriction endonuclease cleavage. TTAGGG repeats introduced at chromosome-internal sites by DNA transfection do not behave as matrix attached loci, suggesting that the telomeric position of the repeats is required for their interaction with the nuclear matrix. These findings are consistent with the idea that telomeres function as a nucleoprotein complex.

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Section: Introductionmentioning

confidence: 85%

Human telomeres are attached to the nuclear matrix.

1992

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“…[43][44][45] To test the possibility that MLL might be associated with the nuclear matrix and chromosomal scaffolds, we used immunofluorescence microscopy to evaluate the relative locations of MLL3AT and topoisomerase II, a major component of the proteinaceous scaffolds. [46][47][48][49] HeLa cells expressing MLL3AT were labeled with ␣-FLAG mAb (fluorescein) and an ␣-topoisomerase II polyclonal antibody (Texas red), and then examined by fluorescence or confocal laser scanning microscopy. By immunofluorescence, the distribution of ␣-FLAG mAb (Figure 4a) and ␣-topoisomerase II pAb (Figure 4b) correlated well in cells in telophase or those undergoing cytokinesis.…”

Section: Mll and Mll3at Associate With Nuclear Matrix And Chromosomalmentioning

confidence: 99%

The amino terminus targets the mixed lineage leukemia (MLL) protein to the nucleolus, nuclear matrix and mitotic chromosomal scaffolds

et al. 2000

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The mixed-lineage leukemia gene (MLL) is associated with more than 25 chromosomal translocations involving band 11q23 in diverse subtypes of human acute leukemia. Conditional expression of a 50 kDa amino terminal fragment spanning the AT hook motifs of MLL (MLL3AT) causes cell cycle arrest, upregulation of p21 Cip1 and p27 Kip1 and partial monocytic differentiation of the monoblastic U937 cell line, suggesting a major role for MLL3AT in MLL-AF9-induced myelomonocytic differentiation. In this study, we analyzed the subcellular localization of conditionally expressed MLL3AT in both U937 and HeLa cell lines. Immunofluorescence staining, confocal laser scanning microscopy and immunoelectron microscopy indicated that MLL3AT, like endogenous MLL, localized in the nucleoplasm in a punctate pattern of distribution, including regions attached to the nuclear envelope and the periphery of the nucleolus. We found that MLL3AT and endogenous MLL were present in interphase nuclear matrices and colocalized with topoisomerase II to mitotic chromosomal scaffolds. Nucleoplasm and nucleolar localization was observed even for MLL-AF9 and MLL-AF4 conditionally expressed chimeric proteins, suggesting a common target conferred by the amino terminus of MLL to many if not all the chimeric MLL proteins. The nuclear matrix/scaffold association suggests a role for the amino terminus of MLL in the modulation of chromatin structure, leading to epigenetic effects on the maintenance of gene expression.

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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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Studies on Scaffold Attachment Sites and Their Relation to Genome Function

Cited by 194 publications

References 167 publications

Human telomeres are attached to the nuclear matrix.

Human telomeres are attached to the nuclear matrix.

The amino terminus targets the mixed lineage leukemia (MLL) protein to the nucleolus, nuclear matrix and mitotic chromosomal scaffolds

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

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