Post-translational histone modifications abound and regulate multiple nuclear processes.
Most modifications are targeted to the amino-terminal domains of histones. Here we report …

The biological significance of recently described modifiable residues in the globular core of
the bovine nucleosome remains elusive. We have mapped these modification sites onto the …

In Saccharomyces cerevisiae, acetylation of lysine 56 (Lys-56) in the globular domain of
histone H3 plays an important role in response to genotoxic agents that interfere with DNA …

Several recent reports have identified lysine 56 (K56) as a novel site of acetylation in yeast
histone H3. K56 acetylation is predicted to disrupt some of the histone-DNA interactions at …

Histone lysine acetylation is a major mechanism by which cells regulate the structure and
function of chromatin, and new sites of acetylation continue to be discovered. Here we …

Studies into posttranslational modifications of histones, notably acetylation, have yielded
important insights into the dynamic nature of chromatin structure and its fundamental role in …

Acetylation of lysine 56 of histone H3 (H3-Lys-56) occurs in S phase and disappears during
G 2/M phase of the cell cycle. However, it is not clear how this modification is regulated …

The best-characterized acetylation of newly synthesized histone H4 is the diacetylation of
the NH2-terminal tail on lysines 5 and 12. Despite its evolutionary conservation, this pattern …

Transcription in eukaryotes is associated with two major changes in chromatin organization.
Firstly, nucleosomal histones are continuously replaced by new histones, an event that in …

Eukaryotic DNA is packaged into a nucleoprotein structure known as chromatin, which is
comprised of DNA, histones, and nonhistone proteins. Chromatin structure is highly …