Phosphorylation of serine 2 within the RNA polymerase IIC-terminal domain couples transcription and 3 ' end processing
- Authors
- Ahn, Seong Hoon; Kim, Minkyu; Buratowski, Stephen
- Issue Date
- Jan-2004
- Publisher
- Cell Press
- Citation
- Molecular Cell, v.13, no.1, pp.67 - 76
- Indexed
- SCIE
SCOPUS
- Journal Title
- Molecular Cell
- Volume
- 13
- Number
- 1
- Start Page
- 67
- End Page
- 76
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/46623
- DOI
- 10.1016/S1097-2765(03)00492-1
- ISSN
- 1097-2765
- Abstract
- The largest subunit of RNA polymerase 11 contains a unique C-terminal domain important for coupling of transcription and mRNA processing. This domain consists of a repeated heptameric sequence (YSPTSPS) phosphorylated at serines 2 and 5. Serine 5 is phosphorylated during initiation and recruits capping enzyme. Serine 2 is phosphorylated during elongation by the Ctk1 kinase, a protein similar to mammalian Cdk9/ P-TEFb. Chromatin immunoprecipitation was used to map positions of transcription elongation and mRNA processing factors in strains lacking Ctkl1. Ctk1 is not required for association of elongation factors with transcribing polymerase. However, in ctk1Delta strains, the recruitment of polyadenylation factors to 3' regions of genes is disrupted and changes in 3' ends are seen. Therefore, Serine 2 phosphorylation by Ctk1 recruits factors for cotranscriptional 3' end processing in vivo.
- Files in This Item
-
Go to Link
- Appears in
Collections - COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY > ERICA 의약생명과학과 > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/46623)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.