Breaking barriers to transcription elongation
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/nrm1981.pdf
Reference151 articles.
1. Prelich, G. RNA polymerase II carboxy-terminal domain kinases: emerging clues to their function. Eukaryot. Cell 1, 153–162 (2002).
2. Sims, R. J., Belotserkovskaya, R. & Reinberg, D. Elongation by RNA polymerase II: the short and long of it. Genes Dev. 18, 2437–2468 (2004).
3. Boehm, A. K., Saunders, A., Werner, J. & Lis, J. T. Transcription factor and polymerase recruitment, modification, and movement on dhsp70 in vivo in the minutes following heat shock. Mol. Cell. Biol. 23, 7628–7637 (2003).
4. Komarnitsky, P., Cho, E. J. & Buratowski, S. Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription. Genes Dev. 14, 2452–2460 (2000).
5. Morris, D. P., Michelotti, G. A. & Schwinn, D. A. Evidence that phosphorylation of the RNA polymerase II carboxyl-terminal repeats is similar in yeast and humans. J. Biol. Chem. 280, 31368–31377 (2005).
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