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Ectomycorrhizal hyphae structure components of the soil bacterial community for decreased phosphatase production.

Identifieur interne : 002423 ( Main/Corpus ); précédent : 002422; suivant : 002424

Ectomycorrhizal hyphae structure components of the soil bacterial community for decreased phosphatase production.

Auteurs : Denise D. Brooks ; Ronald Chan ; Elizabeth R. Starks ; Sue J. Grayston ; Melanie D. Jones

Source :

RBID : pubmed:21265870

English descriptors

Abstract

Ectomycorrhizal fungi (EMF) provide nutrients to their hosts by means of hyphae that extend beyond nutrient-depleted rhizosphere soil. Soil bacteria may compete with EMF for nutrients or may act synergistically to enhance nutrient supply to hosts. To assess the interactions between hyphae and bacteria, two types of small, sand-filled mesh bags were incubated in a Pseudotsuga menziesii/Betula papyrifera forest. The bags allowed ingrowth by EMF (35-μm mesh) or excluded hyphae (0.5-μm mesh), while allowing migration of soil bacteria. After incubation, bacteria were isolated from bags using a method to enrich for Gram-positive bacteria. Isolates were assayed for phosphatase and N-acetyl glucosaminidase (NAGase) activities to assess the potential to access organic phosphorus and nitrogen. The average phosphatase activities were higher in exclusion than ingrowth bags, while NAGase activities did not differ. Streptomyces isolates, which are expected to be strong competitors and antagonists of EMF, were more prevalent in ingrowth bags and yet had lower phosphatase activities. Furthermore, there were no indications of antagonism between fungi and Streptomyces, as there were no increases in NAGase activities in ingrowth bags. We conclude that fungal hyphae can structure components of the soil bacterial community for decreased extracellular enzyme production.

DOI: 10.1111/j.1574-6941.2011.01060.x
PubMed: 21265870

Links to Exploration step

pubmed:21265870

Le document en format XML

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<name sortKey="Chan, Ronald" sort="Chan, Ronald" uniqKey="Chan R" first="Ronald" last="Chan">Ronald Chan</name>
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<name sortKey="Starks, Elizabeth R" sort="Starks, Elizabeth R" uniqKey="Starks E" first="Elizabeth R" last="Starks">Elizabeth R. Starks</name>
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<term>Mycorrhizae (growth & development)</term>
<term>Nitrogen (metabolism)</term>
<term>Phosphoric Monoester Hydrolases (metabolism)</term>
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<term>RNA, Bacterial (genetics)</term>
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<term>Soil Microbiology (MeSH)</term>
<term>Streptomyces (enzymology)</term>
<term>Streptomyces (genetics)</term>
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<term>Nitrogen</term>
<term>Phosphoric Monoester Hydrolases</term>
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<term>Streptomyces</term>
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<term>Streptomyces</term>
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<term>Hyphae</term>
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<term>Betula</term>
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<div type="abstract" xml:lang="en">Ectomycorrhizal fungi (EMF) provide nutrients to their hosts by means of hyphae that extend beyond nutrient-depleted rhizosphere soil. Soil bacteria may compete with EMF for nutrients or may act synergistically to enhance nutrient supply to hosts. To assess the interactions between hyphae and bacteria, two types of small, sand-filled mesh bags were incubated in a Pseudotsuga menziesii/Betula papyrifera forest. The bags allowed ingrowth by EMF (35-μm mesh) or excluded hyphae (0.5-μm mesh), while allowing migration of soil bacteria. After incubation, bacteria were isolated from bags using a method to enrich for Gram-positive bacteria. Isolates were assayed for phosphatase and N-acetyl glucosaminidase (NAGase) activities to assess the potential to access organic phosphorus and nitrogen. The average phosphatase activities were higher in exclusion than ingrowth bags, while NAGase activities did not differ. Streptomyces isolates, which are expected to be strong competitors and antagonists of EMF, were more prevalent in ingrowth bags and yet had lower phosphatase activities. Furthermore, there were no indications of antagonism between fungi and Streptomyces, as there were no increases in NAGase activities in ingrowth bags. We conclude that fungal hyphae can structure components of the soil bacterial community for decreased extracellular enzyme production.</div>
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