Maf1 抑制 RNA 聚合酶 III 转录的结构基础。
Structural basis for RNA polymerase III transcription repression by Maf1.
机构信息
Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Collaboration for Joint PhD Degree between EMBL and Heidelberg University Faculty of Biosciences, Heidelberg University, Heidelberg, Germany.
出版信息
Nat Struct Mol Biol. 2020 Mar;27(3):229-232. doi: 10.1038/s41594-020-0383-y. Epub 2020 Feb 17.
Maf1 is a conserved inhibitor of RNA polymerase III (Pol III) that influences phenotypes ranging from metabolic efficiency to lifespan. Here, we present a 3.3-Å-resolution cryo-EM structure of yeast Maf1 bound to Pol III, establishing that Maf1 sequesters Pol III elements involved in transcription initiation and binds the mobile C34 winged helix 2 domain, sealing off the active site. The Maf1 binding site overlaps with that of TFIIIB in the preinitiation complex.
Maf1 是 RNA 聚合酶 III（Pol III）的保守抑制剂，它影响的表型范围从代谢效率到寿命。在这里，我们展示了酵母 Maf1 与 Pol III 结合的 3.3Å 分辨率冷冻电镜结构，确定 Maf1 隔离了参与转录起始的 Pol III 元件，并结合了可移动的 C34 翼状螺旋 2 结构域，从而封闭了活性位点。Maf1 的结合位点与起始前复合物中 TFIIIB 的结合位点重叠。
Zotero 插件