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The DNA binding affinity of rat liver nucleoproteins to the α1‐acid glycoprotein gene
Author(s) -
Petrovic Miodrag,
Grigorov Ilijana,
Milosavljevic Tanja,
Bogojevic Desanka
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201343
Subject(s) - nucleoprotein , dna , biochemistry , glycoprotein , gene , chemistry , microbiology and biotechnology , biology
Transcriptional regulation and binding interactions between soluble nucleoproteins and the distal regulatory element (DRE) of the rat α1‐acid glycoprotein (α1‐AGP) gene were examined in the liver of rats during the acute‐phase response. Our results show that the elevation of the α1‐AGP gene transcription activity in acute phase liver relies basically on an increase in the binding‐affinity of the constitutive soluble nucleoproteins with molecular masses 35 and 45 kD, enhancing their capability to bind to the distal regulatory element (DRE) of α1‐AGP gene. On the basis of in vitro phosphorylation/dephosphorylation experiments we discuss that the role of these proteins during α1‐AGP transcription may be dependent on their behavior as phosphoproteins. The 35kD nucleoprotein that displayed an acute‐phase inducible affinity to bind DRE was indentified as a C/EBPβ isoform.