With the increased focus on intrinsically disordered proteins (IDPs) and their large interactomes, the question about their specificity—or more so on their multispecificity—arise …
Highly charged intrinsically disordered proteins are essential regulators of chromatin structure and transcriptional activity. Here we identify a surprising mechanism of molecular …
C Pascal, J Zonszain, O Hameiri, C Gargi-Levi… - Molecular Cell, 2023 - cell.com
Histones shape chromatin structure and the epigenetic landscape. H1, the most diverse histone in the human genome, has 11 variants. Due to the high structural similarity between …
MK Hazra, Y Levy - … of the National Academy of Sciences, 2022 - National Acad Sciences
The association between two intrinsically disordered proteins (IDPs) may produce a fuzzy complex characterized by a high binding affinity, similar to that found in the ultrastable …
Chromatin organization plays a critical role in cellular function by regulating access to genetic information. However, understanding chromatin folding is challenging due to its …
S Portillo-Ledesma, Z Li, T Schlick - Current opinion in structural biology, 2023 - Elsevier
The intricacies of the 3D hierarchical organization of the genome have been approached by many creative modeling studies. The specific model/simulation technique combination …
F Hao, S Kale, S Dimitrov, JJ Hayes - Current opinion in structural biology, 2021 - Elsevier
Considerable progress has been made recently in defining the interactions of linker histones (H1s) within nucleosomes. Major advancements include atomic resolution structures of the …
R Hirano, H Ehara, T Kujirai, T Uejima… - Nature …, 2022 - nature.com
In chromatin, linker histone H1 binds to nucleosomes, forming chromatosomes, and changes the transcription status. However, the mechanism by which RNA polymerase II …
Histones compact and store DNA in both Eukarya and Archaea, forming heterodimers in Eukarya and homodimers in Archaea. Despite this, the folding mechanism of histones …