Bas J. G. E. Pieters

TL;DR: This review illustrates that a striking structural diversity of protein assemblies is present in nature, and describes structure-function relationship studies for selected classes of protein architectures, and highlights the techniques that enable the characterisation of supramolecular protein structures.

TL;DR: Comparison of thermodynamic, structural and computational studies provides experimental and theoretical evidence that reader proteins predominantly recognize trimethyllysine via a combination of favourable cation–π interactions and the release of the high-energy water molecules that occupy the aromatic cage of reader proteins on the association with the trimethllysine side chain.

TL;DR: The results suggest that distinct evolutionary pathways led to the interaction between ATRX and HP1 in mammals and its counterpart LHP1 in plants, resulting in distinct modes of transcriptional regulation.

TL;DR: It is demonstrated that H3 histone that bears trimethyllysine analogs can be further assembled into the octameric histone complex that constitutes the nucleosome and chromatin assemblies.

TL;DR: The examination of trimethyllysine analogues as substrates for human TMLH reveals that the enzyme does hydroxylate substrates other than natural l-trimethyllisine.