Effect of endoplasmic reticulum stress on laccase production and the 26S proteasome activity in the white rot fungus Trametes versicolor

Magdalena Staszczak, Joanna Sajewicz, Shoji Ohga

Research output: Contribution to journalArticle

Abstract

The ubiquitin-proteasome pathway is a major system for degrading intracellular proteins in eukaryotes. It degrades many important proteins involved in signal transduction, cell cycle progression, and in general metabolism, including key metabolic enzymes and transcription factors. In addition, the ubiquitin-proteasome system is responsible for endoplasmic reticulum-associated degradation. Our previous studies have demonstrated the presence of proteasomes in white rot Basidiomycetes and indicated that ubiquitinproteasome-mediated pathway in Trametes versicolor is involved in the regulation of laccase, a main ligninolytic enzyme of this fungus, upon nutrient starvation as well as in response to cadmium exposure. Fungal laccases are useful biocatalysts in a wide range of biotechnological applications. Here, we studied the effects of tunicamycin-induced endoplasmic reticulum stress on laccase activity and the 26S proteasomemediated proteolysis in nitrogen-sufficient and nitrogen-deprived cultures of T. versicolor. We found that short-term ER stress (6 h) leads to inhibition of both laccase activity and the 26S proteasome activity. This effect was more pronounced in the nitrogen-deprived cultures. However, after prolonged ER stress (24 h) laccase activity in tunicamycin-treated cultures recovered to levels comparable to those of untreated cultures. In contrast to what was observed after short-term stress, a 24-h tunicamycin treatment resulted in a significant increase in the 26S proteasome activity detected in mycelia from nitrogen-sufficient and nitrogen-deprived cultures (approximately 1.5-fold and 2-fold increase, respectively). Moreover, we found that blocking of proteasome function in T. versicolor subjected to prolonged ER stress resulted in a decrease of laccase activity. These findings suggest a potential role of the proteasome-mediated degradation as an important mechanism by which laccase is regulated under prolonged ER stress.

Original languageEnglish
Pages (from-to)205-211
Number of pages7
JournalJournal of the Faculty of Agriculture, Kyushu University
Volume56
Issue number2
Publication statusPublished - Sep 1 2011

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Trametes
Coriolus versicolor
Laccase
white-rot fungi
Endoplasmic Reticulum Stress
laccase
proteasome endopeptidase complex
endoplasmic reticulum
Fungi
Proteasome Endopeptidase Complex
tunicamycin
Nitrogen
Tunicamycin
nitrogen
ubiquitin
Ubiquitin
Enzymes
Endoplasmic Reticulum-Associated Degradation
Basidiomycota
degradation

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Agronomy and Crop Science

Cite this

Effect of endoplasmic reticulum stress on laccase production and the 26S proteasome activity in the white rot fungus Trametes versicolor. / Staszczak, Magdalena; Sajewicz, Joanna; Ohga, Shoji.

In: Journal of the Faculty of Agriculture, Kyushu University, Vol. 56, No. 2, 01.09.2011, p. 205-211.

Research output: Contribution to journalArticle

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