Structure of a transcribing Pol II-DSIF-SPT6-U1 snRNP complex
Luojia ZhangiD, Christopher BattersiD, Shintaro AibaraiD, Yuliya GordiyenkoiD, Kristina ŽumeriD, Jana SchmitzováiD, Kerstin C. Maier, Patrick CrameriD, Suyang ZhangiD
Abstract
RNA polymerase II (Pol II) facilitates co-transcriptional splicing by recruiting the U1 small nuclear ribonucleoprotein particle (U1 snRNP) to the nascent transcripts. Here, we report the cryo-electron microscopy structure of a transcribing Pol II-U1 snRNP complex with elongation factors DSIF and SPT6. Furthermore, our biochemical analysis revealed that the phosphorylated Pol II carboxyl-terminal domain and SPT6 interact directly with U1 snRNP proteins, facilitating its recruitment to the elongation complex. This multivalent interaction allows efficient spliceosome assembly and ensures transcription processivity.
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