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转录的结构基础:通过在RNA聚合酶II活性中心旋转来选择核酸
Kenneth D Westover1, David A Bushnell, Roger D Kornberg
1Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Cell
|November 13, 2004
概括
RNA聚合酶II使用一种新的核酸选择的两步机制,涉及在活性部位之前的进入部位. 这一发现重新定义了对大型多子单元RNA聚合酶的理解.
科学领域:
- 分子生物学分子生物学
- 结构生物学 结构生物学
- 生物化学 生物化学
背景情况:
- RNA聚合酶II对于真核生物的基因转录至关重要.
- 了解核酸选择的精确机制是调节基因表达的关键.
研究的目的:
- 阐明由RNA聚合酶II进行核酸选择的机制.
- 描述核酸结合和结合的结构基础.
主要方法:
- 使用X射线晶体学可视化RNA聚合酶II转录复合体.
- 对酶内的核酸结合点和方向的分析.
主要成果:
- 揭示了一种两步核酸选择机制,涉及一个进入点 (E) 和一个添加点 (A).
- 不匹配的核酸在潜在旋转之前在E位点以反向的方向结合.
- 第三个核酸结合部位可能调节RNA回溯;DNA解之前的活跃中心.
结论:
- 这些发现为大型多子单元RNA聚合酶中核酸选择建立了新的范式,与单个子单元酶不同.
- 这项研究为RNA聚合酶II的功能和调节提供了原子水平的见解.
- 高分辨率晶体学推进了对酶动态和DNA相互作用的理解.
相关概念视频
Bacterial RNA Polymerase
Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
Eukaryotic RNA Polymerases
RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
All three eukaryotic RNAPs require specific transcription factors, of which the...
RNA Polymerase II Accessory Proteins
Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
Transcription Initiation
Initiation is the first step of transcription in eukaryotes. Prokaryotic RNA Polymerase (RNAP) can bind to the template DNA and start transcribing. On the other hand, transcription in eukaryotes requires additional proteins, called transcription factors, to first bind to the promoter region in the DNA template. This binding helps recruit the specific RNAP that can assemble on the DNA and start transcription.
The promoters and enhancers and their accessory proteins allow tight regulation of...
The promoters and enhancers and their accessory proteins allow tight regulation of...
Bacterial RNA Polymerase
Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
Eukaryotic RNA Polymerases
RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
All three eukaryotic RNAPs require specific transcription factors, of which the...

