Histone acetyltransferases (HATs) directly link chromatin modification to gene activation.
Recent structure/function studies provide insights into HAT catalysis and histone binding …

▪ Abstract Transcriptional regulation in eukaryotes occurs within a chromatin setting and is
strongly influenced by nucleosomal barriers imposed by histone proteins. Among the well …

Over the past 10 years, the study of histone acetyltransferases (HATs) has advanced
significantly, and a number of HATs have been isolated from various organisms. It emerged …

The role of histone acetylation as a key mechanism of transcriptional regulation has been
well established. Recent advances suggest that histone acetyltransferases also play …

Histone acetylation regulates many cellular processes, and specific acetylation marks, either
singly or in combination, produce distinct outcomes. For example, the acetylation pattern on …

Hat1 is the sole known example of a type B histone acetyltransferase. While it has long been
presumed that type B histone acetyltransferases participate in the acetylation of newly …

Protein kinases catalyze phosphorylation, a posttranslational modification widely utilized in
cell signaling. Histone acetyltransferases (HATs) catalyze a counterpart posttranslational …

Histone acetylation has been recognized as an important post‐translational modification of
core nucleosomal histones that changes access to the chromatin to allow gene transcription …

Although histone acetylation has historically been linked to transcription activation, recent
studies indicate that this modification and the enzymes that catalyze it have much broader …

Background: In eukaryotic cells, newly synthesized histone H4 is acetylated at lysines 5 and
12, a transient modification erased by deacetylases shortly after deposition of histones into …