The N terminal transactivation domain of p53 is regulated by ligases and coactivator proteins. The functional conformation of this region appears to be an alpha helix which is necessary for its appropriate interactions with several proteins including MDM2 and p300. Folding simulation studies have been ...
To stimulate the transcription of (a gene in a host cell) by binding to DNA. Genes can be transactivated naturally by a virus or cellular protein or artificially by the insertion of a transactivator gene and segment of DNA into a cell. ...
www.nature.com/scientificreports OPEN The C‑terminal transactivation domain of MITF interacts promiscuously with co‑activator CBP/p300 Alexandra D. Brown , Kyle Lynch & David N. Langelaan * The microphthalmia-associated transcription factor (MITF) is one of four ...
A second isoform, BCCIPβ, sharing an N-terminal acidic domain and a central conserved domain but with a distinct C-terminal domain, also interacts with BRCA2 and p21 (13, 14). Previous studies have suggested a functional role of BCCIP in homologous recombinational repair and G1/S cell ...
The N-terminal domain of p53 is natively unfolded J. Mol. Biol., 332 (2003), pp. 1131-1141 View PDFView articleView in ScopusGoogle Scholar De Mol et al., 2016 E. De Mol, R.B. Fenwick, C.T. Phang, V. Buzon, E. Szulc, A. de la Fuente, A. Escobedo, J. Garcia, C.W....
The transactivation function of the NTM domain did not require homo-trimerization. We also discovered that the NTM domain can be sumoylated at three lysine residues (K123, K208, and K276), with K276 serving as the main acceptor. K276 sumoylation repressed the transactivation function of the...
Department of Biological Sciences, Columbia University, New York, New York. Abstract Cancer-relevant mutations in the oligomerization domain (OD) of the p53 tumor suppressor protein, unlike those in the DNA binding domain, have not been well elucidated. Here, we ...
Through various mechanisms, stress signaling pathways attenuate the activity of key p53 repressors, most prominently MDM2 and MDM4. Both repressors inhibit p53 activity by obstructing its N-terminus transactivating domain, but only MDM2 promotes p53 degradation by the ubiquitin-dependent proteasome5,6...
of MdmX, amino acids 128-444 appears to possess the repressive domain. While an in vivo association of MdmX with either E2F1 or DP1 was not observed, a slight reduction in DP1 and an increased cytoplasmic localization of E2F1 were seen in cells overexpressing MdmX. These results suggest that ...
Results with GAL4 fusion proteins and a synthetic promoter containing GAL4 DNA binding sites indicated that exon2 does not contribute to the HIV-2 Tat activation domain. These observations suggest that exon2 of HIV-2 Tat contributes to transactivation of the HIV-2 LTR by increasing the binding...