FEBS Letters Special Issues: order and disorder
3D Genome Structure – Organization of the nucleus in space and time
Recent advances in 3D genome analyses have shown that chromosomes are structured in space. The genomes of metazoans are segmented in Topologically Associated Domains (TADs), which are highly conserved in their position among cell types and even among species. What TADs actually look like is presently unknown. This FEBS Letters Special Issue, coordinated by Miguel Beato, Victor Corces and Wilhelm Just, addresses topics such as structural and functional diversity of TADs, TADs as dynamic units for gene regulation, architectural hallmarks of the pluripotent genome, structural organization of human replication timing domains, localization of Lamina Associated Domains (LADs) predominantly harboring silent genes, and the forces underlying gene shuttling within chromosomes. Researchers in this field set out to explore eukaryotic 3D genome structure to gain new insights on cellular transcription and differentiation.
3D Genome structure: Organization of the nucleus in space and time (2015) FEBS Lett 589 (20), 2867–3036
Dynamics, flexibility, and intrinsic disorder in protein assemblies
Intrinsically disordered proteins (IDPs) and protein regions (IDPRs) at a first glance may appear to be simpler than their structured companions. However, nothing seems to be simple about disordered proteins. A common trait of IDPs and IDPRs is their structural heterogeneity distinguished by different combinations of foldons (independent foldable units), inducible foldons, non-foldons, semi-foldons and unfoldons, ensuing a remarkable functional pleiotropy. IDPs and IDPRs contribute to protein pliability and, by being promiscuous binders, are constantly involved in various interactions, adopt different folds at interactions sites and play key roles in protein–protein interaction networks. These and other aspects related to IDPs and IDPRs are reviewed in this FEBS Letters Special Issue edited by Vladimir Uversky and Wilhelm Just, in order to provide researchers with the state of the art in this intriguing field of molecular life sciences.
Dynamics, flexibility, and intrinsic disorder in protein assemblies (2015) FEBS Lett 589 (19), 2431–2660