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関連する概念動画

tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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...

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関連する実験動画

Updated: May 29, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

単純なアミノアシルトランスファーゼ基板を用いたN端タンパク質の改変.

Anne M Wagner1, Mark W Fegley, John B Warner

  • 1Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, United States.

Journal of the American Chemical Society
|September 8, 2011
PubMed
まとめ

この研究は,Escherichia coli aminoacyl tRNA transferase (AaT) が,N端のタンパク質改変のために単純なアデノシン基板を効率的に使用できることを示しています. これは,タンパク質の折り畳みを維持しながら,タンパク質工学のための基板の範囲と反応スケールを拡張します.

さらに関連する動画

An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity
07:46

An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity

Published on: October 8, 2018

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

関連する実験動画

Last Updated: May 29, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity
07:46

An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity

Published on: October 8, 2018

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

科学分野:

  • バイオケミストリー バイオケミストリー
  • プロテイン工学は,タンパク質の
  • 合成生物学 合成生物学とは

背景:

  • エシェリキア・コライのアミノアシルtRNAトランスファーゼ (AaT) は,tRNAまたはオリゴヌクレオチドドナーを使用してタンパク質N-ターミンを改変します.
  • N末端タンパク質改変の現在の方法は,基板の制限と複雑な合成に直面しています.

研究 の 目的:

  • AaTの最小限のアデノシン基板をN端タンパク質改変に使用する能力を実証する.
  • 既存のタンパク質改変技術の限界を克服するために.

主な方法:

  • 新型アミノアシルアデノシルドナーによるAaT酵素活性に関する特徴.
  • 簡単に入手可能な材料から最小限のアデノシン基板の合成.
  • AaT活性に対する反応製品の阻害の評価.

主要な成果:

  • AaTは,N端末改変のために最小限のアデノシン基板を効率的に使用します.
  • アデノシルドナーは1〜2つのステップで合成されます.
  • 反応製品は AaT 活動を阻害しません.
  • この方法は,合成酵素の制限と複雑なオリゴヌクレオチド合成を回避します.

結論:

  • アデノシルドナーは,AAT媒介のN端タンパク質改変のための基板の範囲と反応スケールを大幅に改善します.
  • このアプローチは,タンパク質の折り畳みを保存する条件下でタンパク質工学を容易にする.
  • 簡素化された基板合成は,タンパク質の機能研究のためのよりアクセシブルな方法を提供します.