Xem trước tài liệu

Đang tải tài liệu...

Thông tin chi tiết tài liệu

Định dạng: PDF
Số trang: 12 trang
Dung lượng: 232 KB

Giới thiệu nội dung

Investigating RNA Polymerase II Carboxyl-Terminal Domain (CTD) Phosphorylation

Authors: Benoît Palancade and Olivier Bensaude

Affiliation: Génétique Moléculaire, UMR 8541 CNRS, Ecole Normale Supérieure, Paris, France

Field: Molecular Biology, Biochemistry

Document Summary:
This review article explores the phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (RNAP II), a crucial event in mRNA metabolism. It details how enzymes like cell cycle-dependent kinases and TFIIF-dependent phosphatases target the CTD. The repetitive nature of the CTD poses challenges for traditional biochemical analysis, but a panel of monoclonal antibodies has been developed to distinguish between phosphorylated isoforms of RNAP II. The article reviews the successful application of these antibodies in monitoring RNAP II phosphorylation changes in vivo using immunofluorescence, chromatin immunoprecipitation, and immunoblotting. It discusses how CTD phosphorylation patterns are dynamically modified during transcription and their involvement in the sequential recruitment of RNA processing factors. Furthermore, the review examines how global RNAP II phosphorylation is influenced by physiological contexts such as cellular stress and embryonic development.

Detailed Table of Contents:

  • Introduction to RNAP II CTD phosphorylation
  • Keywords
  • The CTD structure and its phosphorylation
  • Multiple RNAP II phosphoisoforms
  • Phosphorylation-dependent epitopes within the CTD
  • Limitations in epitope data interpretation
  • Amino acid residues targeted by CTD-kinases in vitro
  • Transcription factors influence phosphorylation site preference
  • Amino acid residues targeted by CTD-phosphatases
  • Changes in RNAP II phosphorylation along gene transcription
  • Global changes in RNAP II phosphorylation
  • Serine 2 phosphorylation (H5) as a landmark of transcribing RNAP II
  • Conclusion
  • Acknowledgements
  • References