Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
Initiation of Translation02:33

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
Initiation of Translation02:33

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Different modes of engagement with the nucleosome acidic patch yield distinct functional outcomes.

Nucleic acids research·2026
Same author

A DNA damage-activated kinase phosphorylates a transcriptional repressor to control bacterial immune pathway expression.

The EMBO journal·2026
Same author

Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome.

Nature communications·2026
Same author

A natural depsipeptide antibiotic binds the E-site of the bacterial ribosome.

Nature·2026
Same author

Diverse mechanisms of translation arrest by a Clostridia ribosome stalling peptide CliM.

Nature communications·2026
Same author

Discovering New Jumbo Phage Biology with Cryo-Electron Microscopy.

Annual review of virology·2026

関連する実験動画

Updated: Jun 18, 2026

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA
10:15

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA

Published on: July 6, 2012

新生ポリペプチド鎖媒介によるトランスレーションストールに関する構造的洞察.

Birgit Seidelt1, C Axel Innis, Daniel N Wilson

  • 1Gene Center and Center for Integrated Protein Science Munich (CIPSM), Department for Chemistry and Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.

Science (New York, N.Y.)
|November 26, 2009
PubMed
まとめ
この要約は機械生成です。

Escherichia coliのトリプトファナゼオペロン発現中のリボソームの停滞は極めて重要です. リボソームの脱出トンネル内の新生TnaCペプチド相互作用は,放出因子結合部位を変更することによって,翻訳を阻害する.

さらに関連する動画

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
09:42

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Published on: June 19, 2012

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics
09:52

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics

Published on: September 15, 2020

関連する実験動画

Last Updated: Jun 18, 2026

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA
10:15

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA

Published on: July 6, 2012

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
09:42

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Published on: June 19, 2012

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics
09:52

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics

Published on: September 15, 2020

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
  • 微生物学 微生物学とは

背景:

  • バクテリアにおける遺伝子発現の調節は,細胞機能にとって極めて重要です.
  • Escherichia coliのトリプトファナゼオペロンの発現は,TnaCリーダーペプチドの翻訳によって制御されます.
  • TnaC翻訳中のリボソームの停滞は,重要な規制メカニズムです.

研究 の 目的:

  • TnaCリーダーペプチドトランスレーション中のリボソームの停滞の構造的基礎を解明する.
  • リボソームの脱出トンネル内の新生連鎖相互作用が翻訳をどのように調節するかを理解する.
  • 遅滞が翻訳を阻害するメカニズムを調査する.

主な方法:

  • クリオ電子顕微鏡 (cryo-EM) で 5.8 アングストームの解像度.
  • 停止したリボソームの単粒子の再構築.
  • 新生連鎖-リボソーム相互作用の構造分析.

主要な成果:

  • tnaCリーダー遺伝子翻訳中に停滞したリボソームの構造を決定しました.
  • TnaCの誕生鎖とリボソームの出口トンネルとの間の特定の接触を特定しました.
  • 解放因子結合を防ぐペプチジルトランスフェラーゼ中心の構造変化を観察した.
  • 新生鎖がリボソームの出口トンネル内で異なる形状を採用することを示した.

結論:

  • リボソームの脱出トンネル内の新生連鎖相互作用は,翻訳の調節に極めて重要です.
  • トンネル相互作用がペプチジルトランスフェラーゼセンターに信号を送り,翻訳を阻害するモデルが提案されています.
  • リボソーム内の新生鎖の構成はダイナミックで,規制的な役割を果たします.