抄写(语言学)
发起人
蛋白质亚单位
一般转录因子
噬菌体
生物
分子生物学
转录前起始复合物
转录因子
细胞生物学
化学
遗传学
基因
基因表达
大肠杆菌
哲学
语言学
作者
Ming Zhao,Bo Gao,Aijia Wen,Yu Feng,Yuan‐Qiang Lu
出处
期刊:Structure
[Elsevier]
日期:2023-08-01
卷期号:31 (8): 968-974.e3
被引量:4
标识
DOI:10.1016/j.str.2023.05.008
摘要
The CII protein of bacteriophage λ activates transcription from the phage promoters PRE, PI, and PAQ by binding to two direct repeats that straddle the promoter −35 element. Although genetic, biochemical, and structural studies have elucidated many aspects of λCII-mediated transcription activation, no precise structure of the transcription machinery in the process is available. Here, we report a 3.1-Å cryo-electron microscopy (cryo-EM) structure of an intact λCII-dependent transcription activation complex (TAC-λCII), which comprises λCII, E. coli RNAP-σ70 holoenzyme, and the phage promoter PRE. The structure reveals the interactions between λCII and the direct repeats responsible for promoter specificity and the interactions between λCII and RNAP α subunit C-terminal domain responsible for transcription activation. We also determined a 3.4-Å cryo-EM structure of an RNAP-promoter open complex (RPo-PRE) from the same dataset. Structural comparison between TAC-λCII and RPo-PRE provides new insights into λCII-dependent transcription activation.
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