Deciphering the architecture and interactome of the spliceosomal C complex using in vivo chemical crosslinking

ABSTRACT: We used in vivo PIR-based crosslinking to assess specific regions of interaction and protein structure of the spliceosomal C complex components hnRNPA1, A2/B1, and C, and the RALY protein. Our results indicate the interaction of proteins of the C complex via domains regions and conserved motifs, posing as evidence of a coordinated action of known regulatory sequences of RBPs. Moreover, the crosslinking information helped to model some of the RBPs, being complementary to other structural methods available.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Cervix Carcinoma

SUBMITTER: Helisa Wippel  

LAB HEAD: James Bruce

PROVIDER: PXD023577 | Pride | 2022-10-13

REPOSITORIES: Pride