Abstract
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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Acute-Phase Reaction*
-
Animals
-
Blotting, Western
-
DNA-Binding Proteins / chemistry
-
DNA-Binding Proteins / physiology
-
Electrophoresis, Gel, Two-Dimensional
-
Gene Expression Regulation
-
Haptoglobins / genetics
-
High Mobility Group Proteins / chemistry
-
High Mobility Group Proteins / immunology
-
High Mobility Group Proteins / physiology*
-
Male
-
Molecular Weight
-
Nuclear Proteins / chemistry
-
Nuclear Proteins / immunology
-
Nuclear Proteins / physiology*
-
Nucleoproteins / chemistry
-
Phosphoproteins / physiology
-
Phosphorylation
-
Rats
Substances
-
DNA-Binding Proteins
-
Haptoglobins
-
High Mobility Group Proteins
-
Nuclear Proteins
-
Nucleoproteins
-
Phosphoproteins