Hopp til hovedinnholdet

Publikasjoner

NIBIOs ansatte publiserer flere hundre vitenskapelige artikler og forskningsrapporter hvert år. Her finner du referanser og lenker til publikasjoner og andre forsknings- og formidlingsaktiviteter. Samlingen oppdateres løpende med både nytt og historisk materiale. For mer informasjon om NIBIOs publikasjoner, besøk NIBIOs bibliotek.

2012

Sammendrag

The GH61 represents the most enigmatic Glycoside Hydrolase Family (GH) regarding putative enzymatic activity and importance in cellulose degradation. Heterobasidion irregulare is a necrotizing pathogen and white rot fungus, causing enormous damages in conifer forests.The genome of H. irregulare allowed identification of ten HiGH61 genes. qRT-PCR analysis separate the HiGH61 members into two groups; one that show up regulation on lignocellulosic substrates and another that show either down regulation or constitutive expression. This grouping suggests that the fungus relates different sets of GH61s for different substrates, like in the various stages of necrotizing and saprophytic growth on the host.One HiGH61 showed up to 17000 fold increase on spruce heartwood suggesting a pivotal role in cellulose decomposition during saprophytic growth. Sequence analysis of these genes reveals that all GH61s but one possess the conserved metal binding motif predicted to be essential for activity.The sequences also divide into groups having either an insert near the N-terminus or an insert near the second catalytic histidine, which both may represent extensions of the substrate binding surface. Three HiGH61s encode cellulose-binding modules (CBM1), indicating direct targeting of crystalline cellulose, two being up regulated on pure cellulose.There was a common substrate-specific induction patterns of the HiGH61s with several reference cellulolytic and hemicellulolytic GHs, this taken together with their low levels on media lacking lignocellulose, reflect the concerted nature of cell wall polymer degradation.