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
- 46.術中無気肺により発見された気管支型肺平滑筋腫の1例
- 43.経皮的針生検で診断し得た小児肺芽細胞腫の1例
- 問題提起 社会事業と成田山新勝寺 ([地方史研究協議会]大会特集(1)北総地域の水辺と台地--生活空間の歴史的変容)
- 問題提起 北総台地と国策 ([地方史研究協議会]大会特集(1)北総地域の水辺と台地--生活空間の歴史的変容)
- Competitive RT-PCR法によるCD44R1(v8-10)の定量化システムの基礎的検討と臨床応用