A series of investigations proved that acetylation modification plays an important role in regulating SM production via modification of HDACs activities (Albright et al. 2015).
There are two types of methods to predict protein acetylation modification, which are termed as N-terminal Acetylation Prediction and Nε-acetylation Prediction.
However, unlike modifications such as methylations, histone acetylation modifications are often considered redundant.
The HIV-1 transactivator of transcription Tat undergoes multiple posttranslational modifications, including acetylation, methylation, and ubiquitination, which regulate Tat-mediated transactivation of HIV long terminal repeat (LTR) [ 1– 8].
Four core histones H3, H4, H2A, and H2B comprise the nucleosomal core particle, and each may be decorated with multiple covalent modifications, including acetylation, methylation, phosphorylation, sumoylation, and ubiquitination (Kouzarides, 2007).
All the FoxO family proteins are subjected to multiple posttranslational modifications, including phosphorylation, acetylation, methylation, and ubiquitination [ 122].
Histone tails are subject to multiple posttranslational modifications such as acetylation, phosphorylation, ubiquitination, methylation, and poly-ADP-ribosylation, which play a role in transcriptional regulation [ 2- 4].
Recent accounts reveal multiple covalent modifications of p53 protein (phosphorylation, acetylation, ribosylation, sumoylation) that alter its stability and its subcellular localization, as well as affecting its ability to bind DNA and transcriptionally activate target genes [ 20].
Our data also newly reveal multiple sites of modification including N-terminal or S1, K5, K8, K12 and K16 acetylation on H4, N-terminal or S1 acetylation on H1, and T9 and T120 phosphorylation on H2B.
For instance, active promoters are often associated with multiple histone modifications, whereas enhancers are associated with the HATs occupancy and histone acetylation [ 35- 37].
