Abstract
A multiprotein complex isolated from murine cells is identified as a counterpart of the yeast Mediator of transcriptional regulation on the basis of the following: homologs of two subunits of yeast Mediator, Srb7 and Med7, copurify with the complex; peptide sequencing reveals, in addition, homologs of the yeast Mediator subunits Rgr1 and Med6; as with yeast Mediator, the mouse complex binds to the RNA polymerase II C-terminal domain (CTD) and stimulates phosphorylation of the CTD by TFIIH. Peptide sequencing also identifies a component of mouse Mediator as a relative of Ring-3 protein, a mitogen-activated nuclear protein kinase, raising the possibility of Mediator as an end point of signal transduction pathways.
Original language | English (US) |
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Pages (from-to) | 8538-8543 |
Number of pages | 6 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 95 |
Issue number | 15 |
DOIs | |
State | Published - Jul 21 1998 |
Externally published | Yes |
Keywords
- C-terminal domain
- MED genes
- Ring-3
- SRB genes
- TFIIH kinase
ASJC Scopus subject areas
- General