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相关概念视频

Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

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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.
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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
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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.
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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.
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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
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生物分子凝聚物RNase E刺激PNPase活动.

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细菌的核糖蛋白体 (BR体) 通过缩RNase E和多核酸酶 (PNPase) 等酶来增强RNA降解. 这种共同局部化加速PNPase活动,优化细菌中的mRNA衰变.

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科学领域:

  • 细菌分子生物学 细菌分子生物学
  • 生物化学 生物化学
  • RNA代谢的RNA代谢过程

背景情况:

  • 细菌核糖蛋白体 (BR体) 通过相分离组织RNA降解.
  • RNase E和多核酸酶 (PNPase) 是BR体内的mRNA衰变中的关键酶.
  • 以前的研究表明,当PNPase没有被招募到BR体时,RNA衰变中间体会积累.

研究的目的:

  • 为了确定PNPase活动是否在BR体内受到刺激,或者同局部化是否是主要问题.
  • 在体外复制最小的BR体以研究RNase E和PNPase相互作用.
  • 阐明调节细菌RNA衰变的机制.

主要方法:

  • 用PNPase进行RNase E的C终端域的体外复制.
  • 形成最小的BR体 (生物分子凝聚物).
  • 对PNPase催化活性和凝结物中的基质特异性的分析.
  • 研究酸盐对RNase E相分离的影响.

主要成果:

  • 由于脚手架和质量作用,PNPase催化活性在RNase E凝聚物内加速.
  • 扰乱RNase E-PNPase相互作用可以防止招募并降低核糖酶率.
  • RNase E 凝缩物改变PNPase 基质的特异性,使其偏好聚A,而不是聚U.
  • 酸盐抑制RNase E相分离,创建一个反循环.

结论:

  • 通过同局部化和RNase E.的生物分子凝聚剂环境增强PNPase活性.
  • RNase E-PNPase相互作用对于有效的RNA衰变至关重要.
  • 酸盐作为一个调节分子,通过RNase E相分离调整PNPase活性.