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capable of fluorescence resonance energy transfer (FRET). This peptide is known to be a substrate of p300 acetyl-transferase activity (Ott, M. et al. 1999). We shall show that the efficiency of FRET is significantly decreased upon Tat acetylation by p300. Moreover, the choice of this cell-permeable construct allows us to visualize the acetylation states in living cells bypassing cellinvasive procedures. Our results indicate that the sensor can discriminate between basal or altered acetylationdoi:10.1016/j.bpj.2009.12.3167 fatcat:t62fpp74gnfuvphsbzr5yb26em