T-Cell Intracellular Antigen-1 (TIA1) protein is structurally characterized by MAS based solid-state NMR. TIA-1 has a crucial role in cell stress response and stress granule formation in eukaryotes. It contains three RNA Recognition Motifs (RRMs) and a C-terminal low-complexity Prion Related Domain (PRD) that induces amyloid formation under many conditions. A colloid of the protein has been prepared reproducibly without seeding. NMR spectra show excellent homogeneity. Partial assignment of high-dimensional NMR spectra shows that RRM 2 and 3, known to be critically important for function, are folded. Comparison of chemical shifts predicted from homology models and assigned resonances confirm a high degree of similarity to the corresponding truncated domains in solution. In other experiments, the PRD in identical conditions was characterized as an isolated domain and exhibited NMR signals not observed in the full-length protein. These observations support a model for a colloidal form that does not involve amyloid structures. We purpose a model for this multidomain protein wherein the functional domains are well ordered in a solid-like, hydrated phase, and are available for nucleotide binding. By contrast, the PRD and termini of the same protein are disordered and depleted of mobile water. This model features co-localized RNA binding sites and a fluid interior that is reminiscent of stress granules.

Structured RNA recognition motifs in colloidal TIA1 protein

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.