1. Polyadenylation site selection: linking transcription and RNA processing via a conserved carboxy-terminal domain (CTD)-interacting protein
- Author
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Judit Hunyadkürti, Marc Larochelle, and François Bachand
- Subjects
0301 basic medicine ,Polyadenylation ,Transcription, Genetic ,Amino Acid Motifs ,RNA polymerase II ,Cleavage and polyadenylation specificity factor ,Computational biology ,03 medical and health sciences ,MRNA polyadenylation ,Transcription (biology) ,Gene Expression Regulation, Fungal ,Genetics ,RNA Precursors ,RNA, Messenger ,RNA polymerase II holoenzyme ,Binding Sites ,biology ,General Medicine ,biology.organism_classification ,030104 developmental biology ,Schizosaccharomyces pombe ,biology.protein ,RNA Polymerase II ,Schizosaccharomyces pombe Proteins ,Sequence motif ,Protein Binding - Abstract
Despite the fact that the process of mRNA polyadenylation has been known for more than 40 years, a detailed understating of the mechanism underlying polyadenylation site selection is still far from complete. As 3′ end processing is intimately associated with RNA polymerase II (RNAPII) transcription, factors that can successively interact with the transcription machinery and recognize cis-acting sequences on the nascent pre-mRNA would be well suited to contribute to poly(A) site selection. Studies using the fission yeast Schizosaccharomyces pombe have recently identified Seb1, a protein that shares homology with Saccharomyces cerevisiae Nrd1 and human SCAF4/8, and that is critical for poly(A) site selection. Seb1 binds to the C-terminal domain (CTD) of RNAPII via a conserved CTD-interaction domain and recognizes specific sequence motifs clustered downstream of the polyadenylation site on the uncleaved pre-mRNA. In this short review, we summarize insights into Seb1-dependent poly(A) site selection and discuss some unanswered questions regarding its molecular mechanism and conservation.
- Published
- 2016