Premium
Characterization of a nuclear factor that binds to AP1‐like element in the rat p53 promoter during liver regeneration
Author(s) -
Lee Minhyung,
Yu Sunhee,
Park Jongsang
Publication year - 2000
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/1097-4644(20010101)80:1<124::aid-jcb110>3.0.co;2-s
Subject(s) - ap 1 transcription factor , microbiology and biotechnology , biology , binding protein , transcription factor , binding site , activator (genetics) , transcription (linguistics) , gene , biochemistry , linguistics , philosophy
The transcription level of the rat p53 gene increases at 5–12 h in the regenerating liver after partial hepatectomy. It was previously reported that an activator protein 1 (AP1)‐like element (‐264–‐284) mediated the induced transcription of the rat p53 gene during liver regeneration. In this study, we characterize the protein binding to the AP1‐like element by various methods. Oligonucleotide competition assays showed that the binding protein did not require AP1 consensus sequence. Therefore, the binding protein is not an AP1 family protein. Zn 2+ was required for maximum DNA‐binding activity of the protein, suggesting that the binding protein contains zinc fingers. The binding protein was highly resistant to denaturant. Even 1.8 M urea did not eliminate the protein–DNA complexes. In addition, the binding protein was stable up to 55°C. The protein–DNA complexes were abolished in the presence of 0.6 M NaCl and higher. Protease clipping assay showed that the protein had a protease‐resistant core DNA binding domain. These results provided new insights into the structure of the protein that binds to the AP1‐like element of the p53 promoter during liver regeneration. J. Cell. Biochem. 80:124–132, 2000. © 2000 Wiley‐Liss, Inc.