Yi Wei Jiang

TL;DR: 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 Mediation, Srb7 and Med7, copurify with the complex; peptide sequencing reveals a component of mouse Mediator as a relative of Ring-3 protein, a mitogen-activated nuclear protein kinase, raising the possibility of MediatorAs an end point of signal transduction

TL;DR: A similarity in appearance and conformational behavior of yeast and murine complexes indicates a conservation of Mediator structure among eukaryotes.

TL;DR: Findings point to a role of the mediator in repression as well as in transcriptional activation inSin4 and Rgr1 proteins as components of mediator and RNA polymerase II holoenzyme complexes.

TL;DR: Structures of yeast Mediator complex, of a related complex from mouse cells and of thyroid hormone receptor-associated protein complex from human cells have been determined by three-dimensional reconstruction from electron micrographs of single particles.

TL;DR: The results suggest that the sin4 delta mutation may alter the structure of chromatin, and these changes in chromatin structure may affect transcriptional regulation.