Functional mimicry of the acetylated C-terminal tail of p53 by a SUMO-1 acetylated domain, SAD.

ABSTRACT: The ubiquitin-like molecule, SUMO-1, a small protein essential for a variety of biological processes, is covalently conjugated to many intracellular proteins, especially to regulatory components of the transcriptional machinery, such as histones and transcription factors. Sumoylation provides either a stimulatory or an inhibitory signal for proliferation and for transcription, but the molecular mechanisms by which SUMO-1 achieves such versatility of effects are incompletely defined. The tumor suppressor and transcription regulator p53 is a relevant SUMO-1 target. Particularly, the C-terminal tail of p53 undergoes both sumoylation and acetylation. While the effects of sumoylation are still controversial, acetylation modifies p53 interaction with chromatin embedded promoters, and enforces p5

SUBMITTER: Cheema A 

PROVIDER: S-EPMC3614007 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature