Phosphorylation of the C-Terminal Domain of RNA Polymerase II by the Extracellular-Signal-Regulated Protein Kinase ERK2
Rat ERK2, an extracellular-signal-regulated protein kinase family member, phosphorylates RNA polymerase II in vitro. Phosphorylation occurs within the heptapeptide repeats of the C-terminal domain of the largest subunit, in a region important for regulation of transcriptional activity. Analysis of d...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1995-02, Vol.207 (3), p.1051-1057 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Markowitz, R.B. Hermann, A.S. Taylor, D.F. He, L.Y. Anthonycahill, S. Ahn, N.G. Dynan, W.S. |
| description | Rat ERK2, an extracellular-signal-regulated protein kinase family member, phosphorylates RNA polymerase II in vitro. Phosphorylation occurs within the heptapeptide repeats of the C-terminal domain of the largest subunit, in a region important for regulation of transcriptional activity. Analysis of deletion mutants and synthetic peptides showed that ERK2 phosphorylation occurrs at multiple serine residues throughout the C-terminal domain, with no marked preference for consensus repeats versus naturally occurring variants. Our results are consistent with the idea that protein kinases in the extracellular-signal-regulated protein kinase family regulate transcription by direct phosphorylation of RNA polymerase II, but do not support a model where particular portions of the C-terminal domain are special targets of ERK phosphorylation. |
| doi_str_mv | 10.1006/bbrc.1995.1291 |
| format | Article |
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Phosphorylation occurs within the heptapeptide repeats of the C-terminal domain of the largest subunit, in a region important for regulation of transcriptional activity. Analysis of deletion mutants and synthetic peptides showed that ERK2 phosphorylation occurrs at multiple serine residues throughout the C-terminal domain, with no marked preference for consensus repeats versus naturally occurring variants. 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Phosphorylation occurs within the heptapeptide repeats of the C-terminal domain of the largest subunit, in a region important for regulation of transcriptional activity. Analysis of deletion mutants and synthetic peptides showed that ERK2 phosphorylation occurrs at multiple serine residues throughout the C-terminal domain, with no marked preference for consensus repeats versus naturally occurring variants. Our results are consistent with the idea that protein kinases in the extracellular-signal-regulated protein kinase family regulate transcription by direct phosphorylation of RNA polymerase II, but do not support a model where particular portions of the C-terminal domain are special targets of ERK phosphorylation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7864892</pmid><doi>10.1006/bbrc.1995.1291</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1995-02, Vol.207 (3), p.1051-1057 |
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| subjects | Amino Acid Sequence Animals Base Sequence Binding Sites Extracellular Space - enzymology Gene Deletion Glutathione Transferase - genetics Mitogen-Activated Protein Kinase 1 Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism Phosphorylation Protein-Serine-Threonine Kinases - metabolism Protein-Tyrosine Kinases - metabolism Rabbits Rats Recombinant Fusion Proteins - metabolism Repetitive Sequences, Nucleic Acid RNA Polymerase II - chemistry RNA Polymerase II - genetics RNA Polymerase II - metabolism Signal Transduction |
| title | Phosphorylation of the C-Terminal Domain of RNA Polymerase II by the Extracellular-Signal-Regulated Protein Kinase ERK2 |
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