Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways.
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.
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Y W
YW
Jiang
P
P
Veschambre
H
H
Erdjument-Bromage
P
P
Tempst
J W
JW
Conaway
R C
RC
Conaway
R D
RD
Kornberg
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017931:DNA Primers; D056892:Mediator Complex; D051379:Mice; D008969:Molecular Sequence Data; D010766:Phosphorylation; D012319:RNA Polymerase II / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D015534:Trans-Activators / Q000302:isolation & purification / Q000378:metabolism*; D014157:Transcription Factors / Q000302:isolation & purification / Q000378:metabolism
D017931:DNA Primers; C110184:MED7 protein, S cerevisiae; C492153:MED7 protein, human; D056892:Mediator Complex; D011994:Recombinant Proteins; C093965:SRB7 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C490571:Surb7 protein, mouse; D015534:Trans-Activators; D014157:Transcription Factors; D012319:RNA Polymerase II