NSIP

Resources

Title
Enzymatic activities and stable isotope patterns of ectomycorrhizal fungi in relation to phylogeny and exploration types in an afrotropical rain forest
Author(s)
Tedersoo, L.;Naadel, T.;Bahram, M.;Pritsch, K.;Buegger, F.;Leal, M.;Koljalg, U.;Poldmaa, K.
Published
2012
Publisher
New Phytologist
Abstract
Ectomycorrhizal (ECM) fungi obtain both mineral and simple organic nutrients from soil and transport these to plant roots. Natural abundance of stable isotopes (15N and 13C) in fruit bodies and potential enzymatic activities of ECM root tips provide insights into mineral nutrition of these mutualistic partners. By combining rDNA sequence analysis with enzymatic and stable isotope assays of root tips, we hypothesized that phylogenetic affinities of ECM fungi are more important than ECM exploration type, soil horizon and host plant in explaining the differences in mineral nutrition of trees in an African lowland rainforest. Ectomycorrhizal fungal species belonging to extraradical mycelium-rich morphotypes generally displayed the strongest potential activities of degradation enzymes, except for laccase. The signature of 15N was determined by the ECM fungal lineage, but not by the exploration type. Potential enzymatic activities of root tips were unrelated to 15N signature of ECM root tip. The lack of correlation suggests that these methods address different aspects in plant nutrient uptake. Stable isotope analysis of root tips could provide an additional indirect assessment of fungal and plant nutrition that enables enhancement of taxonomic coverage and control for soil depth and internal nitrogen cycling in fungal tissues.
Keywords
13C;15N;degradation enzymes;ectomycorrhiza (ECM) lineages;laccase;nitrogen cycling;N-15 NATURAL-ABUNDANCE;FIELD-COLLECTED FUNGI;SOIL ORGANIC-MATTER;LITTER DECOMPOSITION;MYCORRHIZAL FUNGI;FUNCTIONAL DIVERSITY;SAPROTROPHIC FUNGI;NITROGEN ISOTOPES;PINUS-SYLVESTRIS;GLOBAL PATTERNS

Access Full Text

A full-text copy of this article may be available. Please email the WCS Library to request.




Back

PUB14838