Conserved structures of mediator and RNA polymerase II holoenzyme

被引：212

作者：

Asturias, FJ ^{[1
]}

Jiang, YW ^{[1
]}

Myers, LC ^{[1
]}

Gustafsson, CM ^{[1
]}

Kornberg, RD ^{[1
]}

机构：

[1] Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA

来源：

SCIENCE | 1999年 / 283卷 / 5404期

关键词：

D O I：

10.1126/science.283.5404.985

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 [理学]; 0710 [生物学]; 09 [农学];

摘要：

Single particles of the mediator of transcriptional regulation (Mediator) and of RNA polymerase II holoenzyme were revealed by electron microscopy and image processing. Mediator alone appeared compact, but at high pH or in the presence of RNA polymerase II it displayed an extended conformation. Holoenzyme contained Mediator in a fully extended state, partially enveloping the globular polymerase, with points of apparent contact in the vicinity of the polymerase carboxyl-terminal domain and the DNA-binding channel. A similarity in appearance and conformational behavior of yeast and murine complexes indicates a conservation of Mediator structure among eukaryotes.

引用

页码：985 / 987

页数：3

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