TY  - JOUR
AU  - Poznanović, Goran
AU  - Vidaković, Melita
AU  - Ivanović-Matić, Svetlana
AU  - Martinović, Vesna
PY  - 1999
UR  - http://radar.ibiss.bg.ac.rs/handle/123456789/5640
AB  - 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.
PB  - Hoboken: Wiley
T2  - IUBMB Life
T1  - Identification of nuclear matrix and associated proteins that bind the haptoglobin gene cis-element
IS  - 3
VL  - 48
DO  - 10.1080/713803517
SP  - 277
EP  - 282
ER  - 

@article{
author = "Poznanović, Goran and Vidaković, Melita and Ivanović-Matić, Svetlana and Martinović, Vesna",
year = "1999",
abstract = "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.",
publisher = "Hoboken: Wiley",
journal = "IUBMB Life",
title = "Identification of nuclear matrix and associated proteins that bind the haptoglobin gene cis-element",
number = "3",
volume = "48",
doi = "10.1080/713803517",
pages = "277-282"
}

Poznanović, G., Vidaković, M., Ivanović-Matić, S.,& Martinović, V.. (1999). Identification of nuclear matrix and associated proteins that bind the haptoglobin gene cis-element. in IUBMB Life
Hoboken: Wiley., 48(3), 277-282.
https://doi.org/10.1080/713803517

Poznanović G, Vidaković M, Ivanović-Matić S, Martinović V. Identification of nuclear matrix and associated proteins that bind the haptoglobin gene cis-element. in IUBMB Life. 1999;48(3):277-282.
doi:10.1080/713803517 .

Poznanović, Goran, Vidaković, Melita, Ivanović-Matić, Svetlana, Martinović, Vesna, "Identification of nuclear matrix and associated proteins that bind the haptoglobin gene cis-element" in IUBMB Life, 48, no. 3 (1999):277-282,
https://doi.org/10.1080/713803517 . .

TY  - JOUR
AU  - Martinović, Vesna
AU  - Ivanović-Matić, Svetlana
AU  - Poznanović, Goran
PY  - 1997
UR  - http://radar.ibiss.bg.ac.rs/handle/123456789/5650
AB  - The nuclear matrix, a spherical proteinaceous structure consisting of the peripheral nuclear lamina with nuclear pore complexes, an extensive internal filamentous network and residual nucleoli, is obtained after the extraction of chromatin, soluble proteins and the lipoprotein nuclear membrane.
.DNA loop attachment to the matrix is accomplished through contacts of specific DNA sequences, the matrix association regions (MARs) that delineate different genes and play a role in gene expression (Laemmli et al. 1992; Getzenberg 1994). In addition to MARs, there are other unique sequences on the DNA that likwise bind to the nuclear matrix (Hakes and Berezney 1991). This binding increases  during elevated gene transcription (Brotherton et al. 1991; Sun et al. 1992; Poznanovic et al. 1992; 1994; 1996)
asa result of a remodeling of the thee-dimensional conformation of the points of contact on the matrix due to protein redistribution and posttranslational modifications (Poznanovic et al. 1995; 1996).
PB  - Belgrade: Serbian Biological Society
T2  - Archives of Biological Sciences
T1  - Distribution of the haptoglobin gene 5’ flanking DNA-binding nonhistone proteins in the nuclear matrix
IS  - 1-2
VL  - 49
SP  - 3p
EP  - 4p
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_5650
ER  - 

@article{
author = "Martinović, Vesna and Ivanović-Matić, Svetlana and Poznanović, Goran",
year = "1997",
abstract = "The nuclear matrix, a spherical proteinaceous structure consisting of the peripheral nuclear lamina with nuclear pore complexes, an extensive internal filamentous network and residual nucleoli, is obtained after the extraction of chromatin, soluble proteins and the lipoprotein nuclear membrane.
.DNA loop attachment to the matrix is accomplished through contacts of specific DNA sequences, the matrix association regions (MARs) that delineate different genes and play a role in gene expression (Laemmli et al. 1992; Getzenberg 1994). In addition to MARs, there are other unique sequences on the DNA that likwise bind to the nuclear matrix (Hakes and Berezney 1991). This binding increases  during elevated gene transcription (Brotherton et al. 1991; Sun et al. 1992; Poznanovic et al. 1992; 1994; 1996)
asa result of a remodeling of the thee-dimensional conformation of the points of contact on the matrix due to protein redistribution and posttranslational modifications (Poznanovic et al. 1995; 1996).",
publisher = "Belgrade: Serbian Biological Society",
journal = "Archives of Biological Sciences",
title = "Distribution of the haptoglobin gene 5’ flanking DNA-binding nonhistone proteins in the nuclear matrix",
number = "1-2",
volume = "49",
pages = "3p-4p",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_5650"
}

Martinović, V., Ivanović-Matić, S.,& Poznanović, G.. (1997). Distribution of the haptoglobin gene 5’ flanking DNA-binding nonhistone proteins in the nuclear matrix. in Archives of Biological Sciences
Belgrade: Serbian Biological Society., 49(1-2), 3p-4p.
https://hdl.handle.net/21.15107/rcub_ibiss_5650

Martinović V, Ivanović-Matić S, Poznanović G. Distribution of the haptoglobin gene 5’ flanking DNA-binding nonhistone proteins in the nuclear matrix. in Archives of Biological Sciences. 1997;49(1-2):3p-4p.
https://hdl.handle.net/21.15107/rcub_ibiss_5650 .

Martinović, Vesna, Ivanović-Matić, Svetlana, Poznanović, Goran, "Distribution of the haptoglobin gene 5’ flanking DNA-binding nonhistone proteins in the nuclear matrix" in Archives of Biological Sciences, 49, no. 1-2 (1997):3p-4p,
https://hdl.handle.net/21.15107/rcub_ibiss_5650 .

TY  - JOUR
AU  - Poznanović, Goran
AU  - Martinović, Vesna
AU  - Ivanović-Matić, Svetlana
AU  - Šekularac, Snežana
PY  - 1996
UR  - http://radar.ibiss.bg.ac.rs/handle/123456789/5642
AB  - It was previously shown that during the acute-phase response-induced elevated transcription of the rat haptoglobin gene, protein p55 and the lamins mediate the increased binding of restriction fragment II (-541/-146) via a 38 bp adenine tract lying 147 bp upstream from the haptoglobin gene cis element (-165/-56), to scaffold type II-like nuclear matrices. Here we show that the fragment II binding pattern to > or = 40 kDa proteins of nuclear matrices analogous to type I scaffolds is more complex. Fragment II bound conspicuously to a 40 and less so to p55, a 60 kDa protein and the lamins of control matrices. During increased gene transcription, it bound prominently to p55, the lamins, and less so to 45 and 52 kDa proteins. This was accompanied by the tenacious binding of the DNA to isolated nuclear matrices in vitro and post-translational modifications of certain matrix proteins. The lamins and p55 demonstrated a greater N-acetylglucosamine/sialic acid content and p55 an increased in vitro phosphorylation by a nuclear matrix-associated cyclic-nucleotide-independent kinase. The acute-phase response also caused an increased partitioning of p55 with the nuclear matrix. It was concluded that, as a result of a molecular remodelling of the nuclear matrix at the point of contact with chromatin, the nature of its association with region II DNA changed during elevated haptoglobin gene expression.
PB  - Hoboken: Wiley
T2  - Cell Biology International
T1  - Properties of nuclear matrix proteins that bind the 5' flanking region of the haptoglobin gene are changed during the acute phase response
IS  - 11
VL  - 20
DO  - 10.1006/cbir.1996.0097
SP  - 751
EP  - 762
ER  - 

@article{
author = "Poznanović, Goran and Martinović, Vesna and Ivanović-Matić, Svetlana and Šekularac, Snežana",
year = "1996",
abstract = "It was previously shown that during the acute-phase response-induced elevated transcription of the rat haptoglobin gene, protein p55 and the lamins mediate the increased binding of restriction fragment II (-541/-146) via a 38 bp adenine tract lying 147 bp upstream from the haptoglobin gene cis element (-165/-56), to scaffold type II-like nuclear matrices. Here we show that the fragment II binding pattern to > or = 40 kDa proteins of nuclear matrices analogous to type I scaffolds is more complex. Fragment II bound conspicuously to a 40 and less so to p55, a 60 kDa protein and the lamins of control matrices. During increased gene transcription, it bound prominently to p55, the lamins, and less so to 45 and 52 kDa proteins. This was accompanied by the tenacious binding of the DNA to isolated nuclear matrices in vitro and post-translational modifications of certain matrix proteins. The lamins and p55 demonstrated a greater N-acetylglucosamine/sialic acid content and p55 an increased in vitro phosphorylation by a nuclear matrix-associated cyclic-nucleotide-independent kinase. The acute-phase response also caused an increased partitioning of p55 with the nuclear matrix. It was concluded that, as a result of a molecular remodelling of the nuclear matrix at the point of contact with chromatin, the nature of its association with region II DNA changed during elevated haptoglobin gene expression.",
publisher = "Hoboken: Wiley",
journal = "Cell Biology International",
title = "Properties of nuclear matrix proteins that bind the 5' flanking region of the haptoglobin gene are changed during the acute phase response",
number = "11",
volume = "20",
doi = "10.1006/cbir.1996.0097",
pages = "751-762"
}

Poznanović, G., Martinović, V., Ivanović-Matić, S.,& Šekularac, S.. (1996). Properties of nuclear matrix proteins that bind the 5' flanking region of the haptoglobin gene are changed during the acute phase response. in Cell Biology International
Hoboken: Wiley., 20(11), 751-762.
https://doi.org/10.1006/cbir.1996.0097

Poznanović G, Martinović V, Ivanović-Matić S, Šekularac S. Properties of nuclear matrix proteins that bind the 5' flanking region of the haptoglobin gene are changed during the acute phase response. in Cell Biology International. 1996;20(11):751-762.
doi:10.1006/cbir.1996.0097 .

Poznanović, Goran, Martinović, Vesna, Ivanović-Matić, Svetlana, Šekularac, Snežana, "Properties of nuclear matrix proteins that bind the 5' flanking region of the haptoglobin gene are changed during the acute phase response" in Cell Biology International, 20, no. 11 (1996):751-762,
https://doi.org/10.1006/cbir.1996.0097 . .

TY  - JOUR
AU  - Poznanović, Goran
AU  - Martinović, Vesna
AU  - Ivanović-Matić, Svetlana
AU  - Ševaljević, Ljiljana
PY  - 1994
UR  - http://radar.ibiss.bg.ac.rs/handle/123456789/5643
AB  - The effect of the acute phase response on the affinity of binding between nuclear matrix proteins and the rat haptoglobin (Hp) gene region was examined. Nuclear matrices isolated from acute phase livers were enriched with the 5' Hp gene flanking region (-705/+159), but not with the spliced, protein-coding sequence. Reassociation experiments with isolated nuclear protein matrix spheres and end-labeled fragments I (-146/+156), II (-146/-541), and III (-541/-705) revealed that the matrix proteins displayed an increased binding potential during the acute phase response for all of the examined regions, this being most pronounced for fragment II. BAL 31 digestion of fragment II showed that the sequence element that was responsible for the increased association with nuclear matrix proteins during the acute phase response was a tract of 38 adenine bases. The DNA region established stable associations with nuclear lamin B (67 kDa, pI 5.7) in the controls, and with lamins A (69 kDa, pI 7.0), B, isoforms of lamin C (62 kDa, pI 6.55-6.95), and a 55-kDa (pI 5.9) polypeptide during the acute phase response. Sequence ABC (-165/-56), which overlaps fragments I and II and represents the Hp cis-acting element, did not bind to the non-histone nuclear matrix proteins.
PB  - Oxford, UK: Oxford University Press
T2  - Journal of Biochemistry
T1  - Regions of the haptoglobin 5' flanking gene sequence show different binding affinities to nuclear matrix proteins during the acute phase response
IS  - 3
VL  - 115
DO  - 10.1093/oxfordjournals.jbchem.a124354
SP  - 422
EP  - 428
ER  - 

@article{
author = "Poznanović, Goran and Martinović, Vesna and Ivanović-Matić, Svetlana and Ševaljević, Ljiljana",
year = "1994",
abstract = "The effect of the acute phase response on the affinity of binding between nuclear matrix proteins and the rat haptoglobin (Hp) gene region was examined. Nuclear matrices isolated from acute phase livers were enriched with the 5' Hp gene flanking region (-705/+159), but not with the spliced, protein-coding sequence. Reassociation experiments with isolated nuclear protein matrix spheres and end-labeled fragments I (-146/+156), II (-146/-541), and III (-541/-705) revealed that the matrix proteins displayed an increased binding potential during the acute phase response for all of the examined regions, this being most pronounced for fragment II. BAL 31 digestion of fragment II showed that the sequence element that was responsible for the increased association with nuclear matrix proteins during the acute phase response was a tract of 38 adenine bases. The DNA region established stable associations with nuclear lamin B (67 kDa, pI 5.7) in the controls, and with lamins A (69 kDa, pI 7.0), B, isoforms of lamin C (62 kDa, pI 6.55-6.95), and a 55-kDa (pI 5.9) polypeptide during the acute phase response. Sequence ABC (-165/-56), which overlaps fragments I and II and represents the Hp cis-acting element, did not bind to the non-histone nuclear matrix proteins.",
publisher = "Oxford, UK: Oxford University Press",
journal = "Journal of Biochemistry",
title = "Regions of the haptoglobin 5' flanking gene sequence show different binding affinities to nuclear matrix proteins during the acute phase response",
number = "3",
volume = "115",
doi = "10.1093/oxfordjournals.jbchem.a124354",
pages = "422-428"
}

Poznanović, G., Martinović, V., Ivanović-Matić, S.,& Ševaljević, L.. (1994). Regions of the haptoglobin 5' flanking gene sequence show different binding affinities to nuclear matrix proteins during the acute phase response. in Journal of Biochemistry
Oxford, UK: Oxford University Press., 115(3), 422-428.
https://doi.org/10.1093/oxfordjournals.jbchem.a124354

Poznanović G, Martinović V, Ivanović-Matić S, Ševaljević L. Regions of the haptoglobin 5' flanking gene sequence show different binding affinities to nuclear matrix proteins during the acute phase response. in Journal of Biochemistry. 1994;115(3):422-428.
doi:10.1093/oxfordjournals.jbchem.a124354 .

Poznanović, Goran, Martinović, Vesna, Ivanović-Matić, Svetlana, Ševaljević, Ljiljana, "Regions of the haptoglobin 5' flanking gene sequence show different binding affinities to nuclear matrix proteins during the acute phase response" in Journal of Biochemistry, 115, no. 3 (1994):422-428,
https://doi.org/10.1093/oxfordjournals.jbchem.a124354 . .