Structural and functional homology between the 29 kD rat liver nucleoprotein and the high mobility group 1 protein.
A 29 kD soluble rat liver nucleoprotein (p29) has increased binding affinity for the hormone responsive element (RE) of the rat haptoglobin (Hp) gene during the acute-phase reaction. In this work the possibility of its structural and functional homology to the high mobility group 1 (HMG1) nonhistone protein constituent of chromatin was examined. The results of two-dimensional gel electrophoresis, Southwestern and Western immunoblot analyses, showed that p29 and HMG1 are homologous protein species. On the basis of in vitro and in vivo phosphorylation/dephosphorylation experiments, we discuss the modulatory role of phosphate groups in view of the structure and function of p29.
Petrović
M
M
Molecular Biology Laboratory, Institute for Biological Research, Belgrade, Yugoslav Federal Republic.
Grigorov
I
I
Milosavljević
T
T
Bogojević
D
D
Sekularac
S
S
Sevaljević
L
L
D000210:Acute-Phase Reaction; D000818:Animals; D015153:Blotting, Western; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000502:physiology; D015180:Electrophoresis, Gel, Two-Dimensional; D005786:Gene Expression Regulation; D006242:Haptoglobins / Q000235:genetics; D006609:High Mobility Group Proteins / Q000737:chemistry / Q000276:immunology / Q000502:physiology*; D008297:Male; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000737:chemistry / Q000276:immunology / Q000502:physiology*; D009698:Nucleoproteins / Q000737:chemistry; D010750:Phosphoproteins / Q000502:physiology; D010766:Phosphorylation; D051381:Rats
D004268:DNA-Binding Proteins; D006242:Haptoglobins; D006609:High Mobility Group Proteins; D009687:Nuclear Proteins; D009698:Nucleoproteins; D010750:Phosphoproteins