@article {48945,
	title = {Structural basis of bacterial transcription activation.},
	journal = {Science (New York, N.Y.)},
	volume = {358},
	year = {2017},
	month = {2017 Nov 17},
	pages = {947-951},
	abstract = {<p>In bacteria, the activation of gene transcription at many promoters is simple and only involves a single activator. The cyclic adenosine 3{\textquoteright},5{\textquoteright}-monophosphate receptor protein (CAP), a classic activator, is able to activate transcription independently through two different mechanisms. Understanding the class I mechanism requires an intact transcription activation complex (TAC) structure at a high resolution. Here we report a high-resolution cryo-electron microscopy structure of an intact Escherichia coli class I TAC containing a CAP dimer, a σ(70)-RNA polymerase (RNAP) holoenzyme, a complete class I CAP-dependent promoter DNA, and a de novo synthesized RNA oligonucleotide. The structure shows how CAP wraps the upstream DNA and how the interactions recruit RNAP. Our study provides a structural basis for understanding how activators activate transcription through the class I recruitment mechanism.</p>
},
	issn = {1095-9203},
	doi = {10.1126/science.aao1923},
	author = {Liu, Bin and Hong, Chuan and Huang, Rick K and Yu, Zhiheng and Steitz, Thomas A}
}
