MED genes;
SRB genes;
Ring-3;
C-terminal domain;
TFIIH kinase;
D O I:
10.1073/pnas.95.15.8538
中图分类号:
O [数理科学和化学];
P [天文学、地球科学];
Q [生物科学];
N [自然科学总论];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
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.
机构:
UNIV MASSACHUSETTS, MED CTR, HOWARD HUGHES MED INST, PROGRAM MOLEC MED, WORCESTER, MA 01605 USAUNIV MASSACHUSETTS, MED CTR, HOWARD HUGHES MED INST, PROGRAM MOLEC MED, WORCESTER, MA 01605 USA
Denis, GV
Green, MR
论文数: 0引用数: 0
h-index: 0
机构:
UNIV MASSACHUSETTS, MED CTR, HOWARD HUGHES MED INST, PROGRAM MOLEC MED, WORCESTER, MA 01605 USAUNIV MASSACHUSETTS, MED CTR, HOWARD HUGHES MED INST, PROGRAM MOLEC MED, WORCESTER, MA 01605 USA
机构:
UNIV MASSACHUSETTS, MED CTR, HOWARD HUGHES MED INST, PROGRAM MOLEC MED, WORCESTER, MA 01605 USAUNIV MASSACHUSETTS, MED CTR, HOWARD HUGHES MED INST, PROGRAM MOLEC MED, WORCESTER, MA 01605 USA
Denis, GV
Green, MR
论文数: 0引用数: 0
h-index: 0
机构:
UNIV MASSACHUSETTS, MED CTR, HOWARD HUGHES MED INST, PROGRAM MOLEC MED, WORCESTER, MA 01605 USAUNIV MASSACHUSETTS, MED CTR, HOWARD HUGHES MED INST, PROGRAM MOLEC MED, WORCESTER, MA 01605 USA