Interplay between in vitro acetylation and phosphorylation of tailless HMGB1 protein

The postsynthetic acetylation of HMGB1 protein and its truncated form affects significantly its properties as “architectural” factor – recognition of bent DNA and bending of short DNA fragments. We created mutants at the target sites (lysines 2 and 81) in the tailless HMGB1 modified by the histone a...

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Veröffentlicht in:	Biochemical and biophysical research communications 2009-02, Vol.380 (1), p.138-142
Hauptverfasser:	Pelovsky, Petar, Pashev, Iliya G., Pasheva, Evdokia
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Animals CBP Histone Acetyltransferases - chemistry Histone Acetyltransferases - metabolism HMGB1 protein HMGB1 Protein - chemistry HMGB1 Protein - genetics HMGB1 Protein - metabolism Lysine - chemistry Lysine - genetics Lysine - metabolism Mutagenesis Phosphorylation PKC Rats Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Deletion Tailless HMGB1 protein
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