Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways Journal Article
| Authors: | Jiang, Y. W.; Veschambre, P.; Erdjument-Bromage, H.; Tempst, P.; Conaway, J. W.; Conaway, R. C.; Kornberg, R. D. |
| Article Title: | Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways |
| 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. |
| Keywords: | signal transduction; protein phosphorylation; sequence analysis; conference paper; protein domain; animal cell; mouse; mammalia; animals; mice; carboxy terminal sequence; phosphorylation; animalia; transcription factors; transcription regulation; amino acid sequence; molecular sequence data; sequence homology, amino acid; amino terminal sequence; saccharomyces cerevisiae; nucleotide sequence; recombinant proteins; murinae; base sequence; trans-activators; saccharomyces cerevisiae proteins; dna primers; sequence homology; rna polymerase ii; tfiih kinase; c-terminal domain; human; priority journal; med genes; ring-3; srb genes |
| Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
| Volume: | 95 |
| Issue: | 15 |
| ISSN: | 0027-8424 |
| Publisher: | National Academy of Sciences |
| Date Published: | 1998-07-21 |
| Start Page: | 8538 |
| End Page: | 8543 |
| Language: | English |
| DOI: | 10.1073/pnas.95.15.8538 |
| PUBMED: | 9671713 |
| PROVIDER: | scopus |
| PMCID: | PMC21111 |
| DOI/URL: | |
| Notes: | Conference Paper -- Export Date: 12 December 2016 -- Source: Scopus |
