関連する実験動画
Updated: May 27, 2026

09:16
Oligopeptide Competition Assay for Phosphorylation Site Determination
Published on: May 18, 2017
リン酸化部位の進化のためのメカニズム
Samuel M Pearlman1, Zach Serber, James E Ferrell
1Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Cell
|November 15, 2011
まとめ
自然は,アスパルテートやグルタミン酸のような酸性残留物からタンパク質のリン酸化部位を進化させた. この進化的戦略は,リン酸化がタンパク質を活性化する方法を説明し,その起源に光を当てます.
科学分野:
- バイオケミストリー バイオケミストリー
- 分子生物学は分子生物学である.
- 進化生物学の進化生物学について
背景:
- タンパク質のリン酸化は,リン酸基の可逆的添加を通じてタンパク質の機能を制御する重要な規制メカニズムです.
- リン酸化は負の電荷を導入し,酸性残留物 (アスパルテート/グルタマート) はこの状態を模倣することができます.
- リン酸化部位の進化的起源は完全に理解されていません.
研究 の 目的:
- タンパク質のリン酸化部位の進化的起源を調査する.
- 酸性残留物がリン酸化部位の前駆体として機能するかどうかを調査する.
- 酸性残留から進化するリン酸化部位の機能的影響を理解する.
主な方法:
- 進化パターンを特定するための比較ゲノミクスアプローチ.
- タンパク質 (DNAトポイソメラーゼII,エノラーゼ,C-Raf) の構造分析は,酸性残留から進化したフォスフォサイトによるものです.
主要な成果:
- 自然がアスパルタ酸とグルタミン酸の残留物からセリン,スレオニン,チロシンのリン酸化部位を進化させることを実証した.
- 構造分析により,塩の架け橋に塩基残留と結合した酸性残留物が発見され,これはリン酸化によって条件付きで回復できる.
- 特定された特定のタンパク質 (DNAトポイソメラーゼII,エノラーゼ,C-Raf) が,この進化の経路を例示しています.
結論:
- 酸性残基からのリン酸化部位の進化は,条件付きタンパク質活性化のためのメカニズムを提供します.
- この発見は,なぜ一部のタンパク質がリン酸化によって活性化されるのかについての論理的根拠を提供します.
- タンパク質のリン酸化の起源と複雑性の理解に貢献します.
関連する概念動画
Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
Amplifying Signals via Enzymatic Cascade
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
