Patterns of Proteins That Associate With p53 or With p53 Binding Sites Present in the Ribosal Gene Cluster and MDM2 (P2) Promoter
Abstract
P53 IS A CELLULAR GUARDIAN OF THE GENOME INTEGRITY AND A KEY PLAYER IN PREVENTING TUMOR FORMATION; P53 MUTATION HAS BEEN IMPLICATED IN SEVERAL TYPES OF CANCER SUCH AS BREAST CANCER. A very important fact in its functioning is how p53 selects which one of its cognate sites to bind and when we think that the differential association of p53 with cellular proteins is a key biochemical event in p53 functioning. By DNA affinity chromatography using the p53 binding site present in the promoter 2 of the MDM2 gene (MDM2 P2-affinity chromatography) and nuclear extract from 3-4 cells, we showed the recruitment of the TATA Binding Protein (TBP) and the transcription factor SP1 to the MDM2 P2. The recruitment of TBP and SPi to MDM2 P2 seems to be p53 dependent because we could not TBP or SPI in the MDM2 P2 elution fractions when we used nuclear extract from 10-1 cells, which do not have p53.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 01, 1998
- Accession Number
- ADA364134
Entities
People
- Maria P. Molina
Organizations
- Hunter College