Structural and functional homology between the 29 kD rat liver nucleoprotein and the high mobility group 1 protein
| Autor: | Petrović M, Desanka Bogojević, Ljiljana Ševaljević, Ilijana Grigorov, Tanja Milosavljević, Sekularac S |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Male
Blotting Western Biology Dephosphorylation Genetics Animals Electrophoresis Gel Two-Dimensional Phosphorylation Acute-Phase Reaction Molecular Biology Gel electrophoresis Haptoglobins Haptoglobin High Mobility Group Proteins Nuclear Proteins General Medicine Protein superfamily Phosphoproteins Molecular biology Rats Chromatin Nucleoprotein DNA-Binding Proteins Molecular Weight Nucleoproteins High-mobility group Gene Expression Regulation Biochemistry biology.protein |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1573-4978 0301-4851 |
| DOI: | 10.1007/bf00424433 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink