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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.

SUBMITTER: Jiang YW 

PROVIDER: S-EPMC21111 | biostudies-literature | 1998 Jul

REPOSITORIES: biostudies-literature

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Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways.

Jiang Y W YW   Veschambre P P   Erdjument-Bromage H H   Tempst P P   Conaway J W JW   Conaway R C RC   Kornberg R D RD  

Proceedings of the National Academy of Sciences of the United States of America 19980701 15


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. Pepti  ...[more]

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