The nuclear matrix: Three-dimensional architecture and protein composition

Capco, David G.; Wan, Katherine M.; Penman, Sheldon

doi:10.1016/0092-8674(82)90446-9

Cited by 433 publications

(276 citation statements)

References 37 publications

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“…Components of the nuclear DAPC associate with the nuclear matrix of HeLa cells Because nuclear matrix has been proposed to be the underlying structural support for subnuclear organization of diverse protein complexes [30,31], we examined whether or not the members of the nuclear Dp71-containing DAPC complex bind to the HeLa nuclear matrix. We obtained nuclear and nuclear matrix protein extracts and in situ nuclear matrix preparations by a sequential high salt extraction procedure previously described [22][23][24][25].…”

Section: Dystrophin Dp71 Forms a Dapc In The Nuclei Of Hela Cellsmentioning

confidence: 99%

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Fuentes-Mera

Rodríguez-Muñóz

González‐Ramírez

et al. 2006

Experimental Cell Research

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, et al.. Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: members of the nuclear DAPC associate with the nuclear matrix.. Experimental Cell Research, Elsevier, 2006, 312 (16) ABSTRACT: Dystrophin is an essential component in the assembly and maintenance of the dystrophinassociated protein complex (DAPC), which includes members of the dystroglycan, syntrophin, sarcoglycan and dystrobrevin protein families. Distinctive complexes have been described in the cell membrane of different tissues and cultured cells. In this work, we report the identification and characterization of a novel DAPC present in the nuclei of HeLa cells, which contains dystrophin Dp71 as a key component. Using confocal microscopy and cell fractionation analyses, we found the presence of Dp71, β-sarcoglycan, β-dystroglycan, α-and β-syntrophin, α1-and β-dystrobrevin and nNOS in the nuclei of HeLa cells. Furthermore, we demonstrated by coimmunoprecipitation experiments that most of these proteins form a complex in the nuclear compartment. Next, we analyze the possible association of the nuclear DAPC with the nuclear matrix. We found the presence of Dp71, β-dystroglycan, nNOS, β-sarcoglycan, α/β syntrophin, α1-dystrobrevin and β-dystrobrevin in the nuclear matrix protein fractions and in situ nuclear matrix preparations from HeLa cells. Moreover, we found that Dp71, β-dystroglycan and β-dystrobrevin co-immunoprecipitated with the nuclear matrix proteins lamin B1 and actin. The association of members of the nuclear DAPC with the nuclear matrix indicates that they may work as scaffolding proteins involved in nuclear architecture.

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Section: Dystrophin Dp71 Forms a Dapc In The Nuclei Of Hela Cellsmentioning

confidence: 99%

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Fuentes-Mera

Rodríguez-Muñóz

González‐Ramírez

et al. 2006

Experimental Cell Research

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“…This structure has been defined In two ways. Morphologically, the structures remaining after extraction of nuclei with salt to remove most histones and other proteins appear to represent a proteinaceous network of fibers as observed by electron microscopy (3)(4)(5), although the composition and morphology of these structures has engendered considerable controversy (6,7).…”

Section: Introductionmentioning

confidence: 99%

The association of transcribed genes with the nuclear matrix ofDrosophilacells during heat shock

1985

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ABSIRACTUsing the transcriptional modulation afforded by heat shock, we found that the association of active genes with the nuclear matrix was not dependent on their level of transcription. Heat shock genes were matrix associated both before heat shock (when transcription was relatively low), and during heat shock (when transcription was greatly Increased). Conversely, the cytoplasmic actin gene was matrix associated during normal growth conditions (when transcription was high) and during heat shock (when transcription was greatly decreased). Removal of greater than 99.7% of nascent RNA during preparation of the matrices did not affect these findings. Detailed examination of the cytoplasmic actin gene revealed that Its matrix association was apparently mediated by multiple Interactions near the 5' end of the gene.

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“…It typically consists of the nuclear lamina, residual nucleoli and an internal fibrogranular matrix network (Capco et al, 1982;Verheijen et al, 1988). A great number of studies (for reviews see Verheijen et al, 1988;Gasser et al, 1989) have led to the conclusion that important nuclear processes like DNA replication (Jackson and Cook, 1986), RNA transcription (Jackson and Cook, 1985 a) and DNA loop attachment (Nelson et al, 1986;Gasser and Laemmli, 1987) are at least transiently associated with the nuclear matrix, although contradictory results have been reported (Roberge et al, 1988).…”

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confidence: 99%

Nuclear matrix of the lower eukaryote Physarum polycephalum and the mammalian epithelial LLC‐PK₁ cell line

Eberharter

Grabher

Gstraunthaler

et al. 1993

European Journal of Biochemistry

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Agarose-encapsulated nuclear matrix preparations of the lower eukaryote Physarum polycephalum and the mammalian renal epithelial LLC-PKJ cell line were analyzed after various experimental protocols with respect to the protein composition. The effect of the mode of deproteinization (2 M NaC1,0.25 M ammonium sulfate or 25 mh4 lithium diiodosalicylate), presence of 2-mercaptoethanol, Ca", Cu2+, chelating agents, the sequence of protein extraction and nuclease digestion, the use of RNase, the temperature at which the experimental manipulations were performed and the use of hypotonic or isotonic conditions was investigated. No significant differences in the final nuclear matrix composition could be observed, regardless of the experimental procedure applied. In Physarum, the major nuclear matrix proteins range over 12-70 kDa with prominent bands at 24, 31, 37 and 45 kDa; the proteins of the matrix in U C -P K J cells extend predominantly over 40-80 kDa.Furthermore, no essential differences in the protein composition could be observed when type I and type I1 nuclear matrices from the highly differentiated LLC-PK, cell line were compared. The same was found for analogous matrix preparations of Physarum. Therefore, in both systems a distinction between type I/II matrix is questionable. Immunoblotting of the matrix preparations with a variety of antibodies against intermediate filament proteins and with antinuclear autoantibodies revealed the presence of intermediate filament proteins as components of the nuclear matrix. We conclude that the nuclear matrix represents a much more stable and reproducible structure than has been proposed so far, largely independent of changes in the preparation protocol.

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The nuclear matrix: Three-dimensional architecture and protein composition

Cited by 433 publications

References 37 publications

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

The association of transcribed genes with the nuclear matrix ofDrosophilacells during heat shock

Nuclear matrix of the lower eukaryote Physarum polycephalum and the mammalian epithelial LLC‐PK₁ cell line

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The nuclear matrix: Three-dimensional architecture and protein composition

Cited by 433 publications

References 37 publications

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

The association of transcribed genes with the nuclear matrix ofDrosophilacells during heat shock

Nuclear matrix of the lower eukaryote Physarum polycephalum and the mammalian epithelial LLC‐PK1 cell line

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Product

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Nuclear matrix of the lower eukaryote Physarum polycephalum and the mammalian epithelial LLC‐PK₁ cell line