Archives of Microbiology

, Volume 130, Issue 1, pp 66–71

Ligninolytic activity of Phanerochaete chrysosporium: Physiology of suppression by NH4+ and l-glutamate

  • Patrick Fenn
  • Suki Choi
  • T. Kent Kirk
Article

DOI: 10.1007/BF00527074

Cite this article as:
Fenn, P., Choi, S. & Kirk, T.K. Arch. Microbiol. (1981) 130: 66. doi:10.1007/BF00527074

Abstract

Previous research showed that addition of nutrient nitrogen to ligninolytic (stationary, nitrogen-starved) cultures of the wood-decomposing basidiomycete Phanerochaete chrysosporium causes a suppression of lignin degradation. The present study examined early effects on nitrogen metabolism that followed addition of NH4+and l-glutamate at concentrations that yield similar patterns of suppression. Both nitrogenous compounds were rapidly assimilated (>80% in 6 h). Both caused an initial 80% or greater increase in the intracellular glutamate pool and had similar effects in increasing the specific activities of NADP- and NAD-glutamate dehydrogenases and glutamine synthetase. Differences between the effects of added NH4+and glutamate showed that suppression was not correlated with intracellular pools of arginine or glutamine, nor was the maintenance of an elevated glutamate pool required to maintain the suppressed state. While a portion of the initial glutamate suppression could be attributed to an effect on central carbon metabolism through glutamate catabolism by NAD-glutamate dehydrogenase, the long term suppression by glutamate and the suppression by NH4+were more specific. Suppression by NH4+or glutamate in the presence or absence of protein synthesis (cycloheximide) followed essentially identical kinetics during 12 h. These results indicate that nitrogen additions cause a biochemical repression of enzymes associated with lignin degradation. Results are consistent with the hypothesis that nitrogen metabolism via glutamate plays a role in initiation of repression.

Key words

Wood decay White-rot fungi Lignin biodegradation Fungus physiology Repression by glutamate Glutamate dehydrogenase Glutamine synthetase Intracellular amino acids 

Non-Standard Abbreviations

DMS

2,2-dimethylsuccinate

TCA

trichloroacetic acid

Copyright information

© Springer-Verlag 1981

Authors and Affiliations

  • Patrick Fenn
    • 1
  • Suki Choi
    • 2
  • T. Kent Kirk
    • 2
  1. 1.Department of Plant PathologyUniversity of ArkansasFayettevilleUSA
  2. 2.Forest Service, Forest Products LaboratoryU.S. Department of AgricultureMadisonUSA

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