The RNA polymerase II C-terminal domain-A new role in spliceosome assembly Journal Article

  


Authors: David, C. J.; Manley, J. L.
Article Title: The RNA polymerase II C-terminal domain-A new role in spliceosome assembly
Abstract: Work over the last two decades has provided a wealth of data indicating that the RNA polymerase II transcriptional machinery can play an important role in facilitating the splicing of its transcripts. In particular, the C-terminal domain of the RNA polymerase II large subunit (CTD) is central in the coupling of transcription and splicing. While this has long been assumed to involve physical interactions between splicing factors and the CTD, few functional connections between the CTD and such factors have been established. We recently used a biochemical approach to identify a splicing factor that interacts directly with the CTD to activate splicing and, in doing so, may play a role in the process of spliceosome assembly. © 2011 Landes Bioscience.
Keywords: protein phosphorylation; promoter region; exon; protein conformation; protein domain; carboxy terminal sequence; protein assembly; protein protein interaction; molecular dynamics; intron; protein interaction; proteomics; gene expression regulation; protein processing; amino terminal sequence; protein purification; chromatin immunoprecipitation; rna translation; binding site; catalysis; spliceosome; biochemistry; rna polymerase ii; phase transition; prp19 complex; c-terminal domain; pre-mrna splicing; u2af; ribozyme
Journal Title: Transcription
Volume: 2
Issue: 5
ISSN: 2154-1264
Publisher: Landes Bioscience  
Date Published: 2011-09-01
Start Page: 227
End Page: 231
Language: English
PROVIDER: scopus
DOI/URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-80053041954&partnerID=40&md5=196c1d400b1886629a491ff42e4ba753
Notes: --- - "Export Date: 2 November 2011" - "Source: Scopus"