Michael J. Hendzel

TL;DR: It is proposed that the singular phosphorylation of the amino-terminus of histone H3 may be involved in facilitating two key functions during mitosis: (1) regulate protein-protein interactions to promote binding of trans-acting factors that “drive” chromatin condensation as cells enter M-phase and (2) coordinate chromatin decondensation associated with M- phase.

TL;DR: What is known about the structures and functions of the family ofPARP enzymes are reviewed, and a series of questions that should be addressed are outlined to guide the rational development of PARP inhibitors as anticancer agents.

TL;DR: It is shown that the catalytic domain of HDAC4 interacts with HDAC3 via the transcriptional corepressor N-CoR/SMRT, which indicates that class II HDACs regulate transcription by bridging the enzymatically active SMRT/N- CoR-HDAC3 complex and select transcription factors independently of any intrinsic HDAC activity.

TL;DR: By determining the kinetics of protein assembly following DNA damage, this study reveals the cooperation between PARP1 and the double strand break sensors MRE11 and NBS1 in the close vicinity of a DNA lesion, which may explain the sensitivity of cancer cells to PARP inhibitors.

TL;DR: The results show that histone H1 exchange in vivo is rapid, occurs through a soluble intermediate, and is modulated by the phosphorylation of a protein or proteins as yet to be determined.