Recent trends in studies of biomolecular phase separation.

Abstract

Biomolecular phase separation has recently attracted broad in-terest, due to its role in the spatiotemporal compartmentalization of living cells. It governs the formation, regulation, and dissociation of biomolecular condensates, which play multiple roles in vivo , from activating specific biochemical reactions to organizing chromatin. Interestingly, biomolecular phase separation seems to be a mainly passive process, which can be ex-plained by relatively simple physical principles and reproduced in vitro with a minimal set of components. This Mini review focuses on our current understanding of the fundamental principles of biomolecular phase separation and the recent progress in the research on this topic.

Crosstalk between protein post-translational modifications and phase separation

“…In some external conditions change, some of the molecules in the multi-component system will be enriched to a specific region of the system, the separation of several phases with different components and structures of the process is called phase separation [ 1 ]. In 2009, Brangwynne et al in their study of the mechanisms of fertilized egg polarization and asymmetric division in Caenorhabditis elegans showed that P granules exhibit liquid-like phase change behavior, including fusion, dropping, and wetting [ 2 ].…”

Biomolecular phase separation through theoretical and computational microscope

“…This review is by no means a complete and thorough review of the field; interested readers may be referred to fuller reviews. [11][12][13][14][15][16][17][18][19] This review rather aims to provide a brief sketch of the field. We start our discussion with a summary of what biomolecular phase separation is.…”

“…As a short addendum, we also discuss recent advances in machine‐learning‐based methods to study biomolecular phase separation. This review is by no means a complete and thorough review of the field; interested readers may be referred to fuller reviews 11–19 . This review rather aims to provide a brief sketch of the field.…”

Condensation of the N-terminal domain of human topoisomerase 1 is driven by electrostatic interactions and tuned by its charge distribution

“…At the molecular level, LLPS is driven by both intraand intermolecular interactions [8], including π-π stacking, cation-π, and electrostatic interactions, among residues termed "stickers" [9]. Conversely, "spacers" elements, such as Gly and polar amino acids, serve to separate sticker residues, facilitating the formation of optimal LLPS interactions [10]. Collectively, sequence-specific motifs and chemical context synergistically govern LLPS [11].…”