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von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination.

http://www.ncbi.nlm.nih.gov/pubmed/12604794

The transition from transcription initiation to elongation involves phosphorylation of the large subunit (Rpb1) of RNA polymerase II on the repetitive carboxyl-terminal domain. The elongating hyperphosphorylated Rpb1 is subject to ubiquitination, particularly in response to UV radiation and DNA-damaging agents. By using computer modeling, we identified regions of Rpb1 and the adjacent subunit 6 of RNA polymerase II (Rpb6) that share sequence and structural similarity with the domain of hypoxia-inducible transcription factor 1 alpha (HIF-1 alpha) that binds von Hippel-Lindau tumor suppressor protein (pVHL). pVHL confers substrate specificity to the E3 ligase complex, which ubiquitinates HIF-alpha and targets it for proteasomal degradation. In agreement with the computational model, we show biochemical evidence that pVHL specifically binds the hyperphosphorylated Rpb1 in a proline-hydroxylation-dependent manner, targeting it for ubiquitination. This interaction is regulated by UV radiation.

Pubmed ID: 12604794 RIS Download

Mesh terms: Amino Acid Motifs | Amino Acid Sequence | Animals | Biotinylation | Blotting, Western | Cell Nucleus | DNA Damage | Ligases | Models, Molecular | Molecular Sequence Data | Oxygen | PC12 Cells | Phosphorylation | Precipitin Tests | Proline | Protein Binding | Protein Structure, Tertiary | RNA Polymerase II | Rats | Sequence Homology, Amino Acid | Software | Substrate Specificity | Tumor Suppressor Proteins | Ubiquitin | Ubiquitin-Protein Ligases | Ultraviolet Rays | Von Hippel-Lindau Tumor Suppressor Protein

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Associated grants

  • Agency: NHLBI NIH HHS, Id: HL66312
  • Agency: PHS HHS, Id: L58687

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