CTD Tyrosine Phosphorylation Impairs Termination Factor Recruitment to RNA Polymerase II
| Autor: | Michael Lidschreiber, Corinna Hintermair, Martin Heidemann, Mai Sun, Patrick Cramer, Elisabeth Kremmer, Amelie Schreieck, Dirk Eick, Andreas Mayer |
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| Rok vydání: | 2012 |
| Předmět: |
Chromatin Immunoprecipitation
Saccharomyces cerevisiae Proteins Termination factor RNA polymerase II Saccharomyces cerevisiae environment and public health chemistry.chemical_compound Transcription (biology) Catalytic Domain RNA polymerase Humans Phosphorylation Multidisciplinary biology Tyrosine phosphorylation Cell biology Elongation factor enzymes and coenzymes (carbohydrates) chemistry Biochemistry biology.protein Tyrosine RNA Polymerase II CTD Transcriptional Elongation Factors Protein Kinases HeLa Cells Peptide Termination Factors |
| Zdroj: | Science |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.1219651 |
| Popis: | Don't Terminate Me! DNA transcription progresses through three phases—initiation, elongation, and termination—of messenger RNA chains. The transcribing enzyme, RNA polymerase (Pol) II, recruits factors that assist in each of these phases. Mayer et al. (p. 1723 ) now show that the C-terminal domain (CTD) of actively elongating Pol II is phosphorylated at conserved tyrosine residues. This modification impairs recruitment of termination factors. Factor exchange on the transcribing polymerase enzyme may be explained by an extended CTD code that is based on differential phosphorylation of the tyrosines and two well-characterized serine residues in the CTD. |
| Databáze: | OpenAIRE |
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