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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): Q Exactive HF

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

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Deciphering the architecture and interactome of hnRNP proteins and enigmRBPs.

Wippel Helisa H HH Fioramonte Mariana M Chavez Juan D JD Bruce James E JE

Molecular omics 20210801 4

RNA-binding proteins (RBPs) have conserved domains and consensus sequences that interact with RNAs and other proteins forming ribonucleoprotein (RNP) complexes. RNPs are involved in the regulation of several cellular processes, including transcription, pre-mRNA splicing, mRNA transport, localization, degradation and storage, and ultimately control of translation. Heterogeneous nuclear ribonucleoproteins (hnRNPs) comprise a family of RBPs that mediate transcription control and nuclear processing ...[more]

PMID: 34017973

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