cellulase and diacetylmonoxime

cellulase has been researched along with diacetylmonoxime* in 1 studies

Other Studies

1 other study(ies) available for cellulase and diacetylmonoxime

Article	Year
The myosin ATPase inhibitor, 2,3-butanedione 2-monoxime, prevents protein secretion by the basidiomycete Coprinopsis cinerea. Biotechnology letters, 2011, Volume: 33, Issue:4 The plant-saprophytic basidiomycete, Coprinopsis cinerea, produces and secretes various cellulases during cellulose degradation as the main extracellular proteins. Although enzymatic characterization of such cellulases has been frequently reported, the mechanism of their secretion remains unclear. This study focused on myosins, actin-based motor proteins, involved in protein secretion in C. cinerea. During cultivation under cellulase-inducing condition, no cellulase activity was observed when the mycelia were treated with 2,3-butanedione 2-monoxime (BDM), a general inhibitor of myosin ATPase. Furthermore, BDM treatment disrupted the localization of the Golgi apparatus, but not that of the endoplasmic reticulum. Three genes encoding myosin-like proteins (CcMyo1, CcMyo2 and CcMyo5) were identified from the C. cinerea genome database. Transcription of these genes was promoted when the fungus was grown under cellulase-inducing condition. Topics: Basidiomycota; Cellulase; Diacetyl; Enzyme Inhibitors; Myosins; Reverse Transcriptase Polymerase Chain Reaction	2011

Article

Year

The myosin ATPase inhibitor, 2,3-butanedione 2-monoxime, prevents protein secretion by the basidiomycete Coprinopsis cinerea.

Biotechnology letters, 2011, Volume: 33, Issue:4

The plant-saprophytic basidiomycete, Coprinopsis cinerea, produces and secretes various cellulases during cellulose degradation as the main extracellular proteins. Although enzymatic characterization of such cellulases has been frequently reported, the mechanism of their secretion remains unclear. This study focused on myosins, actin-based motor proteins, involved in protein secretion in C. cinerea. During cultivation under cellulase-inducing condition, no cellulase activity was observed when the mycelia were treated with 2,3-butanedione 2-monoxime (BDM), a general inhibitor of myosin ATPase. Furthermore, BDM treatment disrupted the localization of the Golgi apparatus, but not that of the endoplasmic reticulum. Three genes encoding myosin-like proteins (CcMyo1, CcMyo2 and CcMyo5) were identified from the C. cinerea genome database. Transcription of these genes was promoted when the fungus was grown under cellulase-inducing condition.

Topics: Basidiomycota; Cellulase; Diacetyl; Enzyme Inhibitors; Myosins; Reverse Transcriptase Polymerase Chain Reaction

2011