Spliceosome specifically associates with CTD phospho-serine 5 isoform of RNA polymerase II to promote co-transcriptional splicing
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ABSTRACT: Co-transcriptional splicing of introns is a defining feature of eukaryotic gene expression. We show that the mammalian spliceosome specifically associates with the S5P CTD isoform of RNA polymerase II (Pol II) as it elongates across spliced exons of protein coding genes, both in human Hela and murine lymphoid cell lines. Immuno-precipitation of MNase digested chromatin with phospho CTD specific antibodies reveals that components of the active spliceosome (both snRNA and proteins) form a specific complex with S5P CTD Pol II. Furthermore a dominant splicing intermediate formed by cleavage at intron 5’ss results in the tethering of upstream exons to this complex at all spliced exons. These are invariably connected to upstream spliced constitutive and less frequently to alternative exons. Finally S5P CTD Pol II accumulates over spliced exons but not adjacent introns. We propose that mammalian splicing employs a rapid, co-transcriptional splicing mechanism based on CTD phosphorylation transitions.
INSTRUMENT(S): LTQ XL
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Epithelial Cell Of Cervix, Hela Cell
DISEASE(S): Cervical Cancer
SUBMITTER: Kenny Rebelo
LAB HEAD: Maria Carmo Fonseca
PROVIDER: PXD008197 | Pride | 2018-10-05
REPOSITORIES: Pride
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