Work

Heterochromatin Protein HP1α Gelation Dynamics Revealed by Solid‐State NMR Spectroscopy

Year: 2019

Type: article

Abstract: Heterochromatin protein 1α (HP1α) undergoes liquid-liquid phase separation (LLPS) and forms liquid droplets and gels in vitro, properties that also appear to be central to its biological function in heterochromatin compaction and regulation. Here we use solid-state NMR spectroscopy to track the conformational dynamics of phosphorylated HP1α during its transformation from the liquid to the gel state. Using experiments designed to probe distinct dynamic modes, we identify regions with varying mobilities within HP1α molecules and show that specific serine residues uniquely contribute to gel formation. The addition of chromatin disturbs the gelation process while preserving the conformational dynamics within individual bulk HP1α molecules. Our study provides a glimpse into the dynamic architecture of dense HP1α phases and showcases the potential of solid-state NMR to detect an elusive biophysical regime of phase separating biomolecules.

Source: Angewandte Chemie International Edition

Authors: Bryce E. Ackermann, Galia T. Debelouchina

Institution: University of California San Diego

Language: English

Topic: Advanced NMR Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences, National Institute of Neurological Disorders and Stroke, National Institute of Biomedical Imaging and Bioengineering

Awards: University of California San Diego Neuroscience Microscopy Imaging Core, G834977060, MOLECULAR BIOPHYSICS TRAINING PROGRAM, G9000019215, G9000240485

OpenAlex ID: W2921460772

FWCI: 3.021

Cites: 36

Cited by: 75

Related to: 10