Identification of Nuclear Matrix and Associated Proteins that Bind the Haptoglobin Gene Cis‐Element

Poznanović, Goran; Vidaković, Melita; Ivanović‐Matić, Svetlana; Grujic, Vesna

doi:10.1080/713803517

Cited by 9 publications

(7 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These ndings are in agreement with the increasing body of evidence demonstrating that different regulatory proteins are components of the nuclear matrix (22,(25)(26)(27)(28)(29)(30)(31)(32). The dynamic interactions of C/EBPa and PCNA with the nuclear matrix during liver development lend further support to the concept that the nuclear matrix facilitates gene expression by concentrating and localizing regulatory proteins near their target sites.…”

Section: Resultssupporting

confidence: 77%

“…Recently we reported an increase in DNA-binding af nity and concentration of the nuclear matrix-bound transcription factor C/EBPb during the acute-phase reaction (22). Given that expression of C/EBPa is induced during development and that it regulates hepatocyte proliferation in newborn mice (9), we pursued the association of C/EBPa with the nuclear matrix.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

Ivanović‐Matić¹,

Dinić²,

Vujošević³

et al. 2000

IUBMB Life

View full text Add to dashboard Cite

SummaryThe protein composition of hepatocyte nuclear matrices was examined in rats from the 16th day of gestation to 75 days after birth (adult). An overall increase in size of the nuclear matrix was accompanied by quantitative and qualitative changes in its protein content. Quantitative changes of the major proteins of the peripheral lamina surrounding the isolated nuclear matrix were detected. By Western analysis we established that in pre-and postnatal nuclear matrices the relative concentrations of lamin C were greater than lamin A. After birth, the relative concentrations of both lamins progressively increased. In the adult nuclear matrix, the concentration of lamin A was greater than lamin C. In contrast, the relative concentrations of lamin B remained unchanged throughout development and growth. The relative concentrations of two nuclear matrix -associated regulatory proteins studied changed with development and growth: transcription factor C/EBP® isoforms, which were detected during the gestation period, increased notably after the rst postnatal day, attaining a maximum at the adult stage; the high concentrations of the proliferating cell nuclear antigen (PCNA) perceptibly decreased after the 21st prenatal day. Changes in the composition of the nuclear matrix protein suggest that this structure coordinates nuclear functioning during cell differentiation.IUBMB Life, 49: 511 -517, 2000 Keywords C/EBPa ; hepatocyte development; lamins; nuclear matrix; PCNA.The nuclear matrix is a proteinaceous structural framework of the nucleus. The isolated matrix has a tripartite structure and

show abstract

Section: Resultssupporting

confidence: 77%

Section: Resultsmentioning

confidence: 99%

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

Ivanović‐Matić¹,

Dinić²,

Vujošević³

et al. 2000

IUBMB Life

View full text Add to dashboard Cite

show abstract

“…It has already been suggested that nonspeci c protein-DNA interactions could be the initial interaction in the process of facilitated location of speci c target sites (34,35). We suggested previously that the nuclear matrix undergoes a three-dimensional readjustment at the point of contact with chromatin during the AP reaction (16). This assumption was based on the observed changes of interaction of the 5 0 region of the haptoglobin gene with nuclear matrix proteins, the posttranslational modi cations of the DNA-binding lamins and p55, and the increased partitioning of p55 on the nuclear matrix.…”

Section: Resultsmentioning

confidence: 99%

“…Also involved in the binding were a nuclear matrix protein designated as p55 and lamins A and C (15). The determining factors for the observed increased af nity were the AP-induced posttranslational glucosylation, phosphorylation, and an increased partitioning of p55 on the nuclear matrix (16). In the present work, we have extended our examination of DNA-binding nuclear matrix proteins to the rat haptoglobin gene hormone-responsive cis-element (17), using an electrophoretic mobility shift assay (EMSA) and nonisotopic identi cation of the formed nucleoprotein complexes by silver staining.…”

Section: Introductionmentioning

confidence: 99%

Identification of Nuclear Matrix and Associated Proteins that Bind the Haptoglobin Gene Cis-Element

Poznanović¹,

Vidaković²,

Ivanović‐Matić³

et al. 1999

International Union of Biochemistry and Molecular Biology: Life

Self Cite

View full text Add to dashboard Cite

To identify the major nuclear matrix proteins that bind to the rat haptoglobin gene cis-element, we isolated a soluble nuclear matrix protein fraction and analysed it by gel retardation. Two major DNA-binding proteins exhibiting different types of protein-DNA interactions were detected: a DNA sequence-specific 32-kDa isoform of transcription factor C/EBP beta, and a nuclear matrix protein p55 that bound to the DNA nonspecifically. During increased transcription of the haptoglobin gene in the course of the acute-phase reaction, the DNA-binding affinities and concentrations of these proteins in the soluble nuclear matrix fraction were increased. These data lend further evidence that the nuclear matrix is an active support structure that localizes gene regulatory proteins and participates in transcriptional regulation.

show abstract

“…Re-electrophoresis was performed to separate and identify the proteins in the nucleoprotein complexes according to their molecular masses by SDS-PAGE [Poznanović et al, 1999]. Two gels were always run simultaneously during EMSA.…”

Section: Re-electrophoretic Analysis Of the Nucleoprotein Complexes Omentioning

confidence: 99%

Regulation of rat haptoglobin gene expression is coordinated by the nuclear matrix

Vidaković¹,

Dinić²,

Grdović³

et al. 2009

J of Cellular Biochemistry

View full text Add to dashboard Cite

Using computer stress-induced duplex destabilization (SIDD) analysis and binding experiments, we identified a S/MAR element (-599/-200 bp) (Hp-S/MAR) adjacent to the cis-element (-165/-56 bp) in the rat haptoglobin gene. We examined its functional interactions with the lamins and lamin-associated proteins in the basal state and during acute-phase (AP) response-induced increased transcription. Colocalization, electrophoretic mobility shift assay (EMSA), and re-electrophoresis of nucleoprotein complexes, South-Western and Western blot analysis and coimmunoprecipitation experiments revealed that the lamins, PARP-1, C/EBP beta, and Hp-S/MAR assembled higher order complexes through direct lamin-Hp-S/MAR and probably PARP-1-Hp-S/MAR interactions although C/EBP beta did not bind to the Hp-S/MAR but established direct interaction with PARP-1. The transition from constitutive to increased haptoglobin gene transcription during the AP response was associated with quantitative and qualitative changes in Hp-S/MAR-protein interactions, respectively, observed as increased association of the lamin(s) with the Hp-S/MAR and as the appearance of a 90 kDa Hp-S/MAR-binding protein. Also, during the AP response the contact between C/EBP beta and PARP-1 established in the basal state was lost. DNA chromatography with the haptoglobin cis-element and Western blot analysis suggests that PARP-1 was a coactivator during constitutive and elevated transcription. The results show that the lamin components of the nuclear matrix form a network of functional, dynamic protein-protein and protein-Hp-S/MAR associations with multiple partners, and underline the involvement of PARP-1 in the regulation of haptoglobin gene transcription. We concluded that the interplay of these interactions fine tunes haptoglobin gene expression to meet the changing requirements of liver cells.

show abstract

Identification of Nuclear Matrix and Associated Proteins that Bind the Haptoglobin Gene Cis‐Element

Cited by 9 publications

References 30 publications

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

Identification of Nuclear Matrix and Associated Proteins that Bind the Haptoglobin Gene Cis-Element

Regulation of rat haptoglobin gene expression is coordinated by the nuclear matrix

Contact Info

Product

Resources

About