Studies On The Interactions Between NIRF And P53

To explore the interactions between nuclear protein Np95-like ring finger protein (NIRF) and P53, immunoprecipitation (IP),GST-pull down, in vitriol ubiquitination assay and protein structure bio-information analysis had been employed. The results shown that: 1, NIRF could interact not only with exogenous P53 but with endogenous P53. Further studies shown that the P53 protein had been ubiquitinated by NIRF. 2. NIRF could interact with P53 in vitro. 3. In vitro ubiquitination assay shown that P53 could be strongly ubiquitinated by NIRF. 4. NIRF protein structure bio-information analysis shown that the site of NIRF be phospholated should be on the Ser/Thr residue. The RING finger motif should be the domain which carried the ligase function. Two Zn2+ iron could give different contributions for the RING finger motif.NIRF interacted with P53 protein and finally ubiquitinated P53 protein suggested that NIRF be a negative regulator of P53. P53 had been revealed to be a take its important functions for arresting cell cycle, promoting apoptosis, and maintaining the stability of genome. Our results...