Conformational dynamics, RNA binding, and phase separation regulate the multifunctionality of rabies virus P protein.

ABSTRACT: RNA viruses encode multifunctional proteins to overcome limited genomic capacity and mediate diverse processes in viral replication and host cell modulation. The rabies virus P gene encodes full-length P1 protein and the truncated isoform, P3, which acquires phenotypes absent from P1, including interactions with cellular membrane-less organelles (MLOs) formed by liquid-liquid phase separation (LLPS). This gain-of-function suggests that isoform multifunctionality arises not only from discrete functions of protein modules/domains, but also from conformational regulation involving interactions of the globular C-terminal domain and N-terminal intrinsically disordered regions (IDRs). The precise mechanisms underlying gain-of-function, however, remain unresolved. Here, we compare the structure a

SUBMITTER: Rawlinson SM 

PROVIDER: S-EPMC12589655 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature