High mobility group protein-1 (HMG-1) is a unique activator of p53

Article Abstract:

Binding of p53 protein to DNA is set off by interaction with covalent and noncovalent modifiers. Identification of a factor from HeLa nuclear extracts that start up p53 CNA binding has been achieved. It was found to be a high-mobility group protein, HMG-1, and belongs to a family of much-conserved chromatin-associated nucleoproteins. Members of the family bend DNA and aid binding of some transcription factors to cognate DNA sequences. Recombinant His-tagged HMG-1 helps in p53 DNA binding in vitro and HMG-1; p53 can interact directly in vitro. HMG-1 is unique as an activator of p53.

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ASF/SF2-regulated CaMKIIdelta alternative splicing temporally reprograms excitation-contraction coupling in cardiac muscle

Article Abstract:

A functional dissection of a prototypical SR protein, ASF/SF2, in the heart is presented. The results validate ASF/SF2 as a fundamental splicing regular in the reprogramming pathway and reveal the central contribution of ASF/SF2-regulated CaMKIIdelta alternative splicing to functioning remodeling in developing heart.

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Why is p53 acetylated?

Article Abstract:

Research findings point out that acetylation of p53 tumor suppressor protein does not play an important role in its DNA binding activity, as such some questions arise as to the purpose of this modification to the protein. Data suggest acetylation aids in the regulation of p53 function such as recruiting HAT.

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