ディスルファイド結合形成に必要なタンパク質の特定 in vivo
J C Bardwell1, K McGovern, J Beckwith
1Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115.
Cell
|November 1, 1991
まとめ
dsbA遺伝子の突然変異は,Escherichia coliにおける二硫化結合形成を阻害する. DsbAタンパク質は,タンパク質の適切な折り畳みに不可欠な in vivo の二酸化硫化物結合の形成を促進します.
科学分野:
- 微生物学 微生物学とは
- 分子生物学は分子生物学である.
- タンパク質生化学 タンパク質生化学
背景:
- ディスルファイド結合は,分泌される多くのタンパク質の安定性と機能に不可欠である.
- エシェリキア・コライは,周辺プラズマにおける効率的な二硫化物結合形成のための特定のメカニズムに依存しています.
研究 の 目的:
- エシェリキア・コライ菌における二硫化結合形成におけるdsbA遺伝子の役割を調査する.
- DsbAタンパク質と,タンパク質の折りたたみにおけるその機能を特徴付ける.
主な方法:
- Escherichia coli.におけるdsbA変異体の遺伝子解析について
- パルスチェイスラベリングと,分泌されるタンパク質のプロテアゼ感受性アッセイ.
- 精製されたDsbAタンパク質の活性に関する生化学的特徴.
主要な成果:
- dsbA変異は,β-ラクタマゼ,アルカリリンフォスファタゼ,OmpAなどの分泌されるタンパク質の二硫化結合形成に重大な欠陥を引き起こす.
- dsbA変異体における二酸化炭素結合が欠けているタンパク質は,折りたたみの中間物質であり,プロテアゼの感受性を示すようです.
- dsbA遺伝子は,二硫化酸化還元酵素と活性部位が同型である周辺プラズマタンパク質 (DsbA) をコードする.
- 精製されたDsbAタンパク質は,インスリン内の二硫化結合を減少させる能力を示した.
結論:
- DsbAタンパク質は,Escherichia coli.でジスルファイド結合形成を促進するために不可欠です.
- DsbAは,細菌の周回プラズマ内の酸化タンパク質の折りたたみ経路における重要な酵素として機能する可能性が高い.
さらに関連する動画
12:16High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
Published on: July 30, 2014
26.3K
09:37Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
Published on: May 2, 2019
9.7K
関連する概念動画
Protein Folding
112.3K
Overview
112.3K
Protein and Protein Structure
71.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
71.5K
Protein Modifications in the RER
5.6K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.6K
Protein Folding
8.8K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.8K
Sulfur Assimilation
554
Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
554
