Effect of Inhibition of Proteasome-Mediated Proteolysis on Ligninolytic Activities of White-Rot Fungi
スポンサーリンク
概要
- 論文の詳細を見る
It has recently been established that most short- and long-lived cellular proteins (80-90%) are degraded by a highly selective non-lysosomal pathway that requires ATP and a large (~2.5 MDa) multisubunit, multicatalytic proteinase complex known as the 26S proteasome. It degrades many important proteins involved in signaling pathway, in cell cycle control, and in general metabolism, including transcription factors and key metabolic enzymes. Here, we demonstrated all distinct proteasome activities: chymotrypsin-like, trypsin-like, and caspase-like (peptidylglutamyl-peptide hydrolyzing) in mycelial extracts of the white-rot fungi Trametes versicolor and Phlebia radiata by monitoring cleavage of three different fluorogenic peptide substrates: Suc-LLVY-MCA, Z-GGR-MCA, Z-LLE-βNA, respectively. We also found that this cleavage was ATP-dependent. Reagents that inhibit proteasome-mediated protein degradation in intact cells have recently become available, including substrate-related peptide aldehydes. These inhibitors are useful tools to demonstrate that a process exhibits proteasome-dependent biochemical regulation. In the present study, we report that in vivo Cbz-LLLal treatment strongly inhibited all tested proteasome activities and affected ligninolytic activities in nutrient deprived cultures of both fungi.
- 2008-10-28
論文 | ランダム
- 第42回 東京モーターショー レポート
- 電子ビーム露光装置の環境適合ステージ開発 : ステージと電磁リニアモータの漏洩磁界対策
- 超電導リニアモーターカーの原理と実用化に向けて
- 第42回 東京モーターショー(続)近未来の新技術が集結 実用化と普及をめざすPHVとEV 商用車編(2)
- 編集長インタビュー 大八木成男氏 帝人社長兼CEO(最高経営責任者) 市場と価値観を共有する (川中・川下戦略の研究 帝人(繊維・樹脂・医薬医療品の製造販売))