Structural modularity of the XIST ribonucleoprotein complex.

ABSTRACT: Long noncoding RNAs are thought to regulate gene expression by organizing protein complexes through unclear mechanisms. XIST controls the inactivation of an entire X chromosome in female placental mammals. Here we develop and integrate several orthogonal structure-interaction methods to demonstrate that XIST RNA-protein complex folds into an evolutionarily conserved modular architecture. Chimeric RNAs and clustered protein binding in fRIP and eCLIP experiments align with long-range RNA secondary structure, revealing discrete XIST domains that interact with distinct sets of effector proteins. CRISPR-Cas9-mediated permutation of the Xist A-repeat location shows that A-repeat serves as a nucleation center for multiple Xist-associated proteins and m⁶A modification. Thus modular arch

SUBMITTER: Lu Z 

PROVIDER: S-EPMC7710737 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature