Structural features of human histone acetyltransferase p300 and its complex with p53

► Full-length p300 protein molecule has been visualized by atomic force microscopy. ► Functionally significant N-terminal and C-terminal regions have been identified. ► Complex between p300 and tumor suppressor protein p53 has been visualized. The protein p300 is a multifunctional transcriptional coactivator that plays pivotal role in several cellular functions. Although structures of several domains have been solved in isolation, the structures of full-length protein (p300 FL) or its complexes with transcription activators are completely unknown. Herein, we applied atomic force microscopy to visualize p300 FL. We found that it is almost prolate ellipsoidal in shape, having several bulges. We further identified the functionally significant N-terminal and C-terminal regions, by applying domain-specific antibodies and found that they are located near one end and centre of the molecule, respectively. Importantly, we have visualized the complex between p300 FL and tumor suppressor protein p53. The relevance of these data in understanding dynamics of p300 during acetylation and transcription will be mentioned. p300 and p53bind by atomic force microscopy (View interaction)