TY  - JOUR
AU  - Uskoković, Aleksandra
AU  - Vidaković, Melita
AU  - Dinić, Svetlana
AU  - Ivanović-Matić, Svetlana
AU  - Martinović, Vesna
AU  - Poznanović, Goran
PY  - 2002
UR  - http://radar.ibiss.bg.ac.rs/handle/123456789/5444
AB  - The greatest part of nuclear C/EBP  (a major 35 kD protein, 30 and 38 kD isoforms) was
observed to partition with the nuclear matrix. Cross-linking experiments with formaldehyde
suggested that the association reflected the in situ juxtapositioning of C/EBP  to nuclear matrix
proteins in isolated nuclei. The association of C/EBP  with the nuclear matrix resisted RNase
and DNase treatment and extraction with protein sulfhydryl reducing agents combined with
high ionic strength salt. C/EBP  displayed a proclivity to extensively reassemble with the
filament-forming nuclear matrix proteins after a cycle of solubilization with urea, followed by its
removal by dialysis. These findings suggest that the C/EBP  moieties were anchored to the
nuclear matrix through hydrophobic protein-protein interactions with the lamins. Subsequent
separation of nuclear matrix-associated C/EBP  into insoluble, reassembling, and soluble
nuclear matrix protein (SNMP) fractions after a cycle of solubilization/reassembly pointed to
the sub-partitioning of C/EBP  on the nuclear matrix. DNA affinity chromatography using the
rat haptoglobin gene cis-element and SNMP revealed the binding of p35 during basal
transcription, and p35 and p30 during elevated haptoglobin gene transcription in the course of
the acute-phase (AP) response. It was concluded that the appearance of cis-element-binding p30
in the SNMP fraction resulted from its increased solubility (decreased hydrophobicity) and
inability to reassociate with the lamins during urea removal. The observed solubility partitioning
of C/EBP  on the nuclear matrix framework could represent a level of control of the general
availability of regulatory proteins for establishing interactions with DNA.
PB  - Elsevier Science Ltd.
T2  - Cell Biology International
T1  - Solubility partitioning of C/EBPβ on the rat hepatocyte nuclear matrix by hydrophobic interactions
IS  - 5
VL  - 26
DO  - 10.1006/cbir.2002.0888
SP  - 451
EP  - 461
ER  - 

@article{
author = "Uskoković, Aleksandra and Vidaković, Melita and Dinić, Svetlana and Ivanović-Matić, Svetlana and Martinović, Vesna and Poznanović, Goran",
year = "2002",
abstract = "The greatest part of nuclear C/EBP  (a major 35 kD protein, 30 and 38 kD isoforms) was
observed to partition with the nuclear matrix. Cross-linking experiments with formaldehyde
suggested that the association reflected the in situ juxtapositioning of C/EBP  to nuclear matrix
proteins in isolated nuclei. The association of C/EBP  with the nuclear matrix resisted RNase
and DNase treatment and extraction with protein sulfhydryl reducing agents combined with
high ionic strength salt. C/EBP  displayed a proclivity to extensively reassemble with the
filament-forming nuclear matrix proteins after a cycle of solubilization with urea, followed by its
removal by dialysis. These findings suggest that the C/EBP  moieties were anchored to the
nuclear matrix through hydrophobic protein-protein interactions with the lamins. Subsequent
separation of nuclear matrix-associated C/EBP  into insoluble, reassembling, and soluble
nuclear matrix protein (SNMP) fractions after a cycle of solubilization/reassembly pointed to
the sub-partitioning of C/EBP  on the nuclear matrix. DNA affinity chromatography using the
rat haptoglobin gene cis-element and SNMP revealed the binding of p35 during basal
transcription, and p35 and p30 during elevated haptoglobin gene transcription in the course of
the acute-phase (AP) response. It was concluded that the appearance of cis-element-binding p30
in the SNMP fraction resulted from its increased solubility (decreased hydrophobicity) and
inability to reassociate with the lamins during urea removal. The observed solubility partitioning
of C/EBP  on the nuclear matrix framework could represent a level of control of the general
availability of regulatory proteins for establishing interactions with DNA.",
publisher = "Elsevier Science Ltd.",
journal = "Cell Biology International",
title = "Solubility partitioning of C/EBPβ on the rat hepatocyte nuclear matrix by hydrophobic interactions",
number = "5",
volume = "26",
doi = "10.1006/cbir.2002.0888",
pages = "451-461"
}

Uskoković, A., Vidaković, M., Dinić, S., Ivanović-Matić, S., Martinović, V.,& Poznanović, G.. (2002). Solubility partitioning of C/EBPβ on the rat hepatocyte nuclear matrix by hydrophobic interactions. in Cell Biology International
Elsevier Science Ltd.., 26(5), 451-461.
https://doi.org/10.1006/cbir.2002.0888

Uskoković A, Vidaković M, Dinić S, Ivanović-Matić S, Martinović V, Poznanović G. Solubility partitioning of C/EBPβ on the rat hepatocyte nuclear matrix by hydrophobic interactions. in Cell Biology International. 2002;26(5):451-461.
doi:10.1006/cbir.2002.0888 .

Uskoković, Aleksandra, Vidaković, Melita, Dinić, Svetlana, Ivanović-Matić, Svetlana, Martinović, Vesna, Poznanović, Goran, "Solubility partitioning of C/EBPβ on the rat hepatocyte nuclear matrix by hydrophobic interactions" in Cell Biology International, 26, no. 5 (2002):451-461,
https://doi.org/10.1006/cbir.2002.0888 . .