Evolution, structure and function of divergent macroH2A1 splice isoforms.

The replacement of replication-coupled histones with non-canonical histone variants provides chromatin with additional properties and contributes to the plasticity of the epigenome. MacroH2A histone variants are counterparts of the replication-coupled histone H2A. They are characterized by a unique tripartite structure, consisting of a histone fold, an unstructured linker, and a globular macrodomain.

Unlocking p53 response elements: DNA shape is the key.

For recognition of specific regulatory sequences in the genome (i.e., response elements, REs), the tumor suppressor protein 53 kDa (p53) exhibits dose-dependent selectivity.

Distinct mechanisms control genome recognition by p53 at its target genes linked to different cell fates.

The tumor suppressor p53 integrates stress response pathways by selectively engaging one of several potential transcriptomes, thereby triggering cell fate decisions (e.g., cell cycle arrest, apoptosis).

Rapid Detection of p53 Acetylation Status in Response to Cellular Stress Signaling.

The posttranslational lysine acetylation of proteins is increasingly appreciated as a key regulatory mechanism in fundamental cellular process such as transcription, cytoskeleton dynamics, metabolic flux, and cell survival/death signaling. As empirical studies are undertaken to dissect the functional importance of specific acetylation events, methods for rapid detection of this modification on individual proteins, in different cellular contexts, is essential. Much like nucleosomal histones, the tumor suppressor protein p53 is acetylated on a number of distinct lysine residues, often with distinct functional consequences.