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関連する概念動画

Eukaryotic RNA Polymerases00:58

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...
Eukaryotic RNA Polymerases00:58

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...
Bacterial RNA Polymerase00:43

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...
Bacterial RNA Polymerase00:43

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...
The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...
The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...

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関連する実験動画

Updated: Jul 8, 2026

DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation
09:26

DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation

Published on: December 29, 2021

RNAポリメラーゼI:多機能分子マシンである.

Jeremy R Haag1, Craig S Pikaard

  • 1Department of Biology, Washington University, 1 Brookings Drive, St. Louis, MO, USA.

Cell
|December 28, 2007
PubMed
まとめ

研究者らは,冷凍電子顕微鏡を用いて酵母RNAポリメラーゼIの構造をマッピングした. これは,RNAポリメラーゼIIが使用するトランスクリプション因子とは異なり,3つのサブユニットがトランスクリプション延長を処理することを明らかにした.

科学分野:

  • 分子生物学は分子生物学である.
  • 構造生物学 構造生物学とは
  • バイオケミストリー バイオケミストリー

背景:

  • イーストRNAポリメラーゼI (Pol I) は,リボソームRNA合成に不可欠です.
  • Pol Iの構造を理解することは,転写におけるその機能を解読する鍵です.
  • Pol Iのこれまでの構造データは,特に,延長中のサブユニット相互作用に関して,限られていた.

研究 の 目的:

  • イーストRNAポリメラーゼI酵素の完全な3次元構造を決定する.
  • 転写延長における特定のサブユニットの役割を解明する.
  • Pol Iの機能的メカニズムと関連するRNAポリメラーゼII (Pol II) システムを比較する.

主な方法:

  • 高解像度画像を取得するために,冷凍電子顕微鏡 (cryo-EM) が採用されました.
  • この研究は,14サブユニットの酵母Pol I酵素に焦点を当てた.
  • 画像処理と構造モデリングを使用して,酵素のアーキテクチャを再構築しました.

主要な成果:

  • 14サブユニットの酵母Pol I酵素の完全な構造は,12 Åの解像度で解明されました.
  • Pol I内の3つの特定のサブユニットは,トランスクリプションの延長に重要な役割を果たしているとして特定されました.

さらに関連する動画

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
10:59

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis
07:38

DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis

Published on: October 6, 2017

関連する実験動画

Last Updated: Jul 8, 2026

DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation
09:26

DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation

Published on: December 29, 2021

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
10:59

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis
07:38

DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis

Published on: October 6, 2017

  • これらの機能は,Pol IIシステムとは異なり,Pol Iサブユニットによって本質的に実行されます.

    • 結論:

    • 構造は,酵母Pol I.内の転写延長のための固有のメカニズムを明らかにします.
    • これは,RNAポリメラーゼI系とRNAポリメラーゼII系の機能メカニズムが異なることを強調している.
    • この発見は,Pol I媒介のrRNA遺伝子転写を理解するための構造的基礎を提供します.