The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain Journal Article
| Authors: | Myers, L. C.; Gustafsson, C. M.; Bushnell, D. A.; Lui, M.; Erdjument-Bromage, H.; Tempst, P.; Kornberg, R. D. |
| Article Title: | The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain |
| Abstract: | Mediator was resolved from yeast as a multiprotein complex on the basis of its requirement for transcriptional activation in a fully defined system. Three groups of mediator polypeptides could be distinguished: the products of five SRB genes, identified as suppressors of carboxy-terminal domain (CTD)- truncation mutants; products of four genes identified as global repressors; and six members of a new protein family, termed Med, thought to be primarily responsible for transcriptional activation. Notably absent from the purified mediator were Srbs 8, 9, 10, and 11, as well as members of the SWI/SNF complex. The CTD was required for function of mediator in vitro, in keeping with previous indications of involvement of the CTD in transcriptional activation in vivo. Evidence for human homologs of several mediator proteins, including Med7, points to similar mechanisms in higher cells. |
| Keywords: | nonhuman; protein domain; animal cell; carboxy terminal sequence; protein protein interaction; enzyme activity; animalia; tumor suppressor gene; saccharomyces cerevisiae; transcription; yeast; protein family; enzyme subunit; rna polymerase ii; repressor gene; mediator release; priority journal; article; ctd; rna polymerase ii holoenzyme |
| Journal Title: | Genes and Development |
| Volume: | 12 |
| Issue: | 1 |
| ISSN: | 0890-9369 |
| Publisher: | Cold Spring Harbor Laboratory Press |
| Date Published: | 1998-01-01 |
| Start Page: | 45 |
| End Page: | 54 |
| Language: | English |
| PUBMED: | 9420330 |
| PROVIDER: | scopus |
| PMCID: | PMC316402 |
| DOI: | 10.1101/gad.12.1.45 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 12 December 2016 -- Source: Scopus |
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