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A widespread mechanism in ectomycorrhizal fungi to access nitrogen from mineral-associated proteins

Wang, Tao LU ; Persson, Per LU and Tunlid, Anders LU (2021) In Environmental Microbiology 23(10). p.5837-5849
Abstract

A large fraction of nitrogen (N) in forest soils is present in mineral-associated proteinaceous compounds. The strong association between proteins and minerals limits microbial accessibility to this source, which is a relatively stable reservoir of soil N. We have shown that the ectomycorrhizal (ECM) fungus Paxillus involutus can acquire N from iron oxide-associated proteins. Using tightly controlled isotopic, spectroscopic and chromatographic experiments, we demonstrated that the capacity to access N from iron oxide-associated bovine serum albumin (BSA) is shared with the ECM fungi Hebeloma cylindrosporum and Piloderma olivaceum. Despite differences in evolutionary history, growth rates, exploration types and the decomposition... (More)

A large fraction of nitrogen (N) in forest soils is present in mineral-associated proteinaceous compounds. The strong association between proteins and minerals limits microbial accessibility to this source, which is a relatively stable reservoir of soil N. We have shown that the ectomycorrhizal (ECM) fungus Paxillus involutus can acquire N from iron oxide-associated proteins. Using tightly controlled isotopic, spectroscopic and chromatographic experiments, we demonstrated that the capacity to access N from iron oxide-associated bovine serum albumin (BSA) is shared with the ECM fungi Hebeloma cylindrosporum and Piloderma olivaceum. Despite differences in evolutionary history, growth rates, exploration types and the decomposition mechanisms of organic matter, their N acquisition mechanisms were similar to those described for P. involutus. The fungi released N from mineral-associated BSA by direct action of extracellular aspartic proteases on the mineral-associated BSA, without initial desorption of the protein. Hydrolysis was suppressed by the adsorption of proteases to minerals, but this adverse effect was counteracted by the secretion of compounds that conditioned the mineral surface. These data suggest that the enzymatic exudate-driven mechanism to access N from mineral-associated proteins is found in ECM fungi of multiple lineages and exploration types.

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organization
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type
Contribution to journal
publication status
published
subject
in
Environmental Microbiology
volume
23
issue
10
pages
5837 - 5849
publisher
Wiley-Blackwell
external identifiers
  • scopus:85105027742
  • pmid:33891367
ISSN
1462-2912
DOI
10.1111/1462-2920.15539
language
English
LU publication?
yes
id
a56c264b-2c94-42e8-82f9-13c70cfeb2f0
date added to LUP
2021-05-31 14:20:51
date last changed
2024-04-20 06:51:34
@article{a56c264b-2c94-42e8-82f9-13c70cfeb2f0,
  abstract     = {{<p>A large fraction of nitrogen (N) in forest soils is present in mineral-associated proteinaceous compounds. The strong association between proteins and minerals limits microbial accessibility to this source, which is a relatively stable reservoir of soil N. We have shown that the ectomycorrhizal (ECM) fungus Paxillus involutus can acquire N from iron oxide-associated proteins. Using tightly controlled isotopic, spectroscopic and chromatographic experiments, we demonstrated that the capacity to access N from iron oxide-associated bovine serum albumin (BSA) is shared with the ECM fungi Hebeloma cylindrosporum and Piloderma olivaceum. Despite differences in evolutionary history, growth rates, exploration types and the decomposition mechanisms of organic matter, their N acquisition mechanisms were similar to those described for P. involutus. The fungi released N from mineral-associated BSA by direct action of extracellular aspartic proteases on the mineral-associated BSA, without initial desorption of the protein. Hydrolysis was suppressed by the adsorption of proteases to minerals, but this adverse effect was counteracted by the secretion of compounds that conditioned the mineral surface. These data suggest that the enzymatic exudate-driven mechanism to access N from mineral-associated proteins is found in ECM fungi of multiple lineages and exploration types.</p>}},
  author       = {{Wang, Tao and Persson, Per and Tunlid, Anders}},
  issn         = {{1462-2912}},
  language     = {{eng}},
  number       = {{10}},
  pages        = {{5837--5849}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Environmental Microbiology}},
  title        = {{A widespread mechanism in ectomycorrhizal fungi to access nitrogen from mineral-associated proteins}},
  url          = {{http://dx.doi.org/10.1111/1462-2920.15539}},
  doi          = {{10.1111/1462-2920.15539}},
  volume       = {{23}},
  year         = {{2021}},
}