Split-APEX implicates splicing factor SRSF1 and splicing helicases in ribosomal biogenesis.

ABSTRACT: SR proteins are RNA-binding proteins with one or two RNA recognition motif (RRM)-type RNA-binding domains and a C-terminal region rich in arginine-serine dipeptides. They function in cellular processes ranging from transcription to translation. The best-known SR protein, SRSF1, modulates RNA splicing by stabilizing the binding of constitutive splicing factors, but there is also evidence that it participates in constitutive splicing reactions and is present in spliceosomal complexes. It has been shown recently that it interacts with DDX23, an RNA helicase that triggers the transition from complex pre-B to complex B during activation of the spliceosome. To identify in which other steps of spliceosome assembly and reaction it might be present, we have used split-APEX with SRSF1 and a number o

SUBMITTER: Paschalis V 

PROVIDER: S-EPMC12757297 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature