Effect of inhibition of proteasome-mediated proteolysis on ligninolytic activities of white-rot fungi

Nam Seok Cho, Magdalena Staszczak, Jerzy Rogalski, Hee Yeon Cho, Shoji Ohga

Research output: Contribution to journalArticle

Abstract

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: chymotrypsinlike, 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-βSNA, 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.

Original languageEnglish
Pages (from-to)399-404
Number of pages6
JournalJournal of the Faculty of Agriculture, Kyushu University
Volume53
Issue number2
Publication statusPublished - Oct 2008
Externally publishedYes

Fingerprint

white-rot fungi
proteasome endopeptidase complex
Proteasome Endopeptidase Complex
proteolysis
Proteolysis
Fungi
peptides
Peptides
Adenosine Triphosphate
Phlebia
Trametes
Coriolus versicolor
caspases
Caspases
protein degradation
Cell Cycle Checkpoints
Fluorescent Dyes
Aldehydes
Trypsin
trypsin

All Science Journal Classification (ASJC) codes

  • Agronomy and Crop Science
  • Biotechnology

Cite this

Effect of inhibition of proteasome-mediated proteolysis on ligninolytic activities of white-rot fungi. / Cho, Nam Seok; Staszczak, Magdalena; Rogalski, Jerzy; Cho, Hee Yeon; Ohga, Shoji.

In: Journal of the Faculty of Agriculture, Kyushu University, Vol. 53, No. 2, 10.2008, p. 399-404.

Research output: Contribution to journalArticle

Cho, Nam Seok ; Staszczak, Magdalena ; Rogalski, Jerzy ; Cho, Hee Yeon ; Ohga, Shoji. / Effect of inhibition of proteasome-mediated proteolysis on ligninolytic activities of white-rot fungi. In: Journal of the Faculty of Agriculture, Kyushu University. 2008 ; Vol. 53, No. 2. pp. 399-404.
@article{03781669bcfc47e5bec65ef728a8d71f,
title = "Effect of inhibition of proteasome-mediated proteolysis on ligninolytic activities of white-rot fungi",
abstract = "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: chymotrypsinlike, 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-βSNA, 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.",
author = "Cho, {Nam Seok} and Magdalena Staszczak and Jerzy Rogalski and Cho, {Hee Yeon} and Shoji Ohga",
year = "2008",
month = "10",
language = "English",
volume = "53",
pages = "399--404",
journal = "Journal of the Faculty of Agriculture, Kyushu University",
issn = "0023-6152",
publisher = "Faculty of Agriculture, Kyushu University",
number = "2",

}

TY - JOUR

T1 - Effect of inhibition of proteasome-mediated proteolysis on ligninolytic activities of white-rot fungi

AU - Cho, Nam Seok

AU - Staszczak, Magdalena

AU - Rogalski, Jerzy

AU - Cho, Hee Yeon

AU - Ohga, Shoji

PY - 2008/10

Y1 - 2008/10

N2 - 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: chymotrypsinlike, 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-βSNA, 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.

AB - 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: chymotrypsinlike, 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-βSNA, 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.

UR - http://www.scopus.com/inward/record.url?scp=57349178535&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=57349178535&partnerID=8YFLogxK

M3 - Article

VL - 53

SP - 399

EP - 404

JO - Journal of the Faculty of Agriculture, Kyushu University

JF - Journal of the Faculty of Agriculture, Kyushu University

SN - 0023-6152

IS - 2

ER -