Thermodynamic stability of hnRNP A1 low complexity domain revealed by high-pressure NMR.

ABSTRACT: We have investigated the pressure- and temperature-induced conformational changes associated with the low complexity domain of hnRNP A1, an RNA-binding protein able to phase separate in response to cellular stress. Solution NMR spectra of the hnRNP A1 low-complexity domain fused with protein-G B1 domain were collected from 1 to 2500 bar and from 268 to 290 K. While the GB1 domain shows the typical pressure-induced and cold temperature-induced unfolding expected for small globular domains, the low-complexity domain of hnRNP A1 exhibits unusual pressure and temperature dependences. We observed that the low-complexity domain is pressure sensitive, undergoing a major conformational transition within the prescribed pressure range. Remarkably, this transition has the inverse temperature dependen

SUBMITTER: Levengood JD 

PROVIDER: S-EPMC9122033 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature