dc.creator | Uskoković, Aleksandra | |
dc.creator | Vidaković, Melita | |
dc.creator | Dinić, Svetlana | |
dc.creator | Ivanović-Matić, Svetlana | |
dc.creator | Martinović, Vesna | |
dc.creator | Poznanović, Goran | |
dc.date.accessioned | 2023-02-07T14:41:35Z | |
dc.date.available | 2900-01-01 | |
dc.date.issued | 2002 | |
dc.identifier.issn | 1065-6995 | |
dc.identifier.uri | http://radar.ibiss.bg.ac.rs/handle/123456789/5444 | |
dc.description.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. | sr |
dc.language.iso | en | sr |
dc.publisher | Elsevier Science Ltd. | sr |
dc.relation | Tthe Research Science Fund of the Serbian Ministry of Science, Contract No. 1722 | sr |
dc.rights | restrictedAccess | sr |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.source | Cell Biology International | sr |
dc.subject | Acute phase (AP) response | sr |
dc.subject | CCAAT/enhancer-binding proteins (C/EBP) α and β | sr |
dc.subject | Haptoglobin gene | sr |
dc.subject | Lamins A/C | sr |
dc.subject | Nuclear matrix | sr |
dc.title | Solubility partitioning of C/EBPβ on the rat hepatocyte nuclear matrix by hydrophobic interactions | sr |
dc.type | article | sr |
dc.rights.license | BY | sr |
dc.rights.holder | ©2002 by Elsevier Science Ltd | sr |
dc.citation.issue | 5 | |
dc.citation.volume | 26 | |
dc.identifier.doi | 10.1006/cbir.2002.0888 | |
dc.identifier.pmid | 12095231 | |
dc.identifier.scopus | 2-s2.0-0035991606 | |
dc.identifier.wos | 000176946900008 | |
dc.citation.spage | 451 | |
dc.citation.epage | 461 | |
dc.type.version | publishedVersion | sr |
dc.citation.rank | M23 | |