scholarly journals Mannitol Metabolism in Agaricus bisporus: Purification and Properties of Mannitol Dehydrogenase

Microbiology ◽  
1985 ◽  
Vol 131 (11) ◽  
pp. 2885-2890 ◽  
Author(s):  
N. MORTON ◽  
A. G. DICKERSON ◽  
J. B. W. HAMMOND
Keyword(s):  
Agaricus Bisporus ◽  
Mannitol Dehydrogenase ◽  
Purification And Properties ◽  
Mannitol Metabolism

Purification and properties of mannitol dehydrogenase from Agaricus bisporus sporocarps

1978 ◽  
Vol 17 (5) ◽  
pp. 865-868 ◽  
Author(s):  
Hans Peter Ruffner ◽  
Dora Rast ◽  
Hanspeter Tobler ◽  
Hans Karesch
Keyword(s):  
Agaricus Bisporus ◽  
Mannitol Dehydrogenase ◽  
Purification And Properties

Cloning and Characterization of NADP-Mannitol Dehydrogenase cDNA from the Button Mushroom, Agaricus bisporus, and Its Expression in Response to NaCl Stress

1998 ◽  
Vol 64 (12) ◽  
pp. 4689-4696 ◽  
Author(s):  
Johan M. H. Stoop ◽  
Hans Mooibroek
Keyword(s):  
Amino Acid ◽  
Agaricus Bisporus ◽  
Fruit Body ◽  
Transcript Level ◽  
Nacl Stress ◽  
Amino Acid Sequences ◽  
Mannitol Dehydrogenase ◽  
Button Mushroom ◽  
Physiological Importance ◽  
Uromyces Fabae

ABSTRACT Mannitol, a six-carbon sugar alcohol, is the main storage carbon in the button mushroom, Agaricus bisporus. Given the physiological importance of mannitol metabolism in growth, fruit body development, and salt tolerance of A. bisporus, the enzyme responsible for mannitol biosynthesis, NADP-dependent mannitol dehydrogenase (MtDH) (EC 1.1.1.138 ), was purified to homogeneity, andMtDH cDNA was cloned, sequenced, and characterized. To our knowledge, this represents the first report on the isolation of a cDNA encoding an NADP-dependent mannitol dehydrogenase. TheMtDH cDNA contains an open reading frame of 789 bp encoding a protein of approximately 28 kDa. The N-terminal and internal amino acid sequences of the deduced protein exactly matched the ones determined from the purified MtDH subunit, whereas the amino acid composition of the deduced protein was nearly identical to that of the purified MtDH. The MtDH cDNA showed high homology with a plant-induced short-chain dehydrogenase from Uromyces fabae. Phylogenetic analysis based on amino acid sequences from mannitol(-1-phosphate) dehydrogenases indicated a close relationship between the substrate specificity of the enzymes and phylogenetic differentiation. Salt-stressed fruit bodies showed an overall increase in mannitol biosynthesis, as was evident from the increase in MtDH activity, MtDH abundance, and MtDH RNA accumulation. Furthermore, the MtDH transcript level seems to be under developmental control, as MtDH RNA accumulated during maturation of the fruit body.

scholarly journals Novel insights into mannitol metabolism in the fungal plant pathogen Botrytis cinerea

2010 ◽  
Vol 427 (2) ◽  
pp. 323-332 ◽  
Author(s):  
Thierry Dulermo ◽  
Christine Rascle ◽  
Geneviève Billon-Grand ◽  
Elisabeth Gout ◽  
Richard Bligny ◽  
...  
Keyword(s):  
Botrytis Cinerea ◽  
Plant Pathogen ◽  
Mannitol Dehydrogenase ◽  
Targeted Deletion ◽  
In Vivo Nmr ◽  
Double Deletion ◽  
Mannitol Metabolism ◽  
Genes Encoding ◽  
Gene Transcripts

In order to redefine the mannitol pathway in the necrotrophic plant pathogen Botrytis cinerea, we used a targeted deletion strategy of genes encoding two proteins of mannitol metabolism, BcMTDH (B. cinerea mannitol dehydrogenase) and BcMPD (B. cinerea mannitol-1-phosphate dehydrogenase). Mobilization of mannitol and quantification of Bcmpd and Bcmtdh gene transcripts during development and osmotic stress confirmed a role for mannitol as a temporary and disposable carbon storage compound. In order to study metabolic fluxes, we followed conversion of labelled hexoses in wild-type and ΔBcmpd and ΔBcmtdh mutant strains by in vivo NMR spectroscopy. Our results revealed that glucose and fructose were metabolized via the BcMPD and BcMTDH pathways respectively. The existence of a novel mannitol phosphorylation pathway was also suggested by the NMR investigations. This last finding definitively challenged the existence of the originally postulated mannitol cycle in favour of two simultaneously expressed pathways. Finally, physiological and biochemical studies conducted on double deletion mutants (ΔBcmpdΔBcmtdh) showed that mannitol was still produced despite a complete alteration of both mannitol biosynthesis pathways. This strongly suggests that one or several additional undescribed pathways could participate in mannitol metabolism in B. cinerea.

scholarly journals Mannitol is required for asexual sporulation in the wheat pathogen Stagonospora nodorum (glume blotch)

2006 ◽  
Vol 399 (2) ◽  
pp. 231-239 ◽  
Author(s):  
Peter S. Solomon ◽  
Ormonde D. C. Waters ◽  
Cordula I. Jörgens ◽  
Rohan G. T. Lowe ◽  
Judith Rechberger ◽  
...  
Keyword(s):  
Double Mutant ◽  
Physiological Role ◽  
Stagonospora Nodorum ◽  
In Planta ◽  
Mannitol Dehydrogenase ◽  
Glume Blotch ◽  
Dehydrogenase Gene ◽  
Mannitol Metabolism ◽  
Mutant Strains

The physiological role of the mannitol cycle in the wheat pathogen Stagonospora nodorum (glume blotch) has been investigated by reverse genetics and metabolite profiling. A putative mannitol 2-dehydrogenase gene (Mdh1) was cloned by degenerate PCR and disrupted. The resulting mutated mdh1 strains lacked all detectable NADPH-dependent mannitol dehydrogenase activity. The mdh1 strains were unaffected for mannitol production but, surprisingly, were still able to utilize mannitol as a sole carbon source, suggesting a hitherto unknown mechanism for mannitol catabolism. The mutant strains were not compromised in their ability to cause disease or sporulate. To further our understanding of mannitol metabolism, a previously developed mannitol-1-phosphate dehydrogenase (gene mpd1) disruption construct [Solomon, Tan and Oliver (2005) Mol. Plant–Microbe Interact. 18, 110–115] was introduced into the mutated mdh1 background, resulting in a strain lacking both enzyme activities. The mpd1mdh1 strains were unable to grow on mannitol and produced only trace levels of mannitol. The double-mutant strains were unable to sporulate in vitro when grown on minimal medium for extended periods. Deficiency in sporulation was correlated with the depletion of intracellular mannitol pools. Significantly sporulation could be restored with the addition of mannitol. Pathogenicity of the double mutant was not compromised, although, like the previously characterized mpd1 mutants, the strains were unable to sporulate in planta. These findings not only question the currently hypothesized pathways of mannitol metabolism, but also identify for the first time that mannitol is required for sporulation of a filamentous fungus.

scholarly journals Regulation of Mannitol Dehydrogenase: Relationship to Plant Growth and Stress Tolerance

HortScience ◽  
1997 ◽  
Vol 32 (3) ◽  
pp. 551F-552
Author(s):  
D.M. Pharr ◽  
R.T.N. Prata ◽  
J.B. Jennings ◽  
J.D. Williamson ◽  
E. Zamski ◽  
...  
Keyword(s):  
Stress Tolerance ◽  
Agricultural Soils ◽  
Plant Diseases ◽  
Mannitol Dehydrogenase ◽  
Hexose Sugars ◽  
Long Run ◽  
Genetically Engineer ◽  
Mannitol Metabolism ◽  
Energy Maintenance

Increasing salinity of agricultural soils may ultimately limit the sustainability of food production in some areas of the world. Work from our laboratory and the labs of others demonstrates that mannitol, a six-carbon sugar alcohol, is important as a stress-related metabolite in some plants. Mannitol helps plants resist the damaging effects of stressful growth environments, such as drought, high soil salinity, and perhaps attack by microorganisms that cause plant diseases. In the long run, we hope to genetically engineer plants to produce and use mannitol for increased productivity and tolerance to environmental stresses. Basic information about how plants regulate those genes important to mannitol metabolism is of critical importance to this long-term goal. Our laboratory discovered an enzyme, mannitol dehydrogenase, that is the first critical biochemical step in mannitol use in vascular plants. Later, we cloned the gene for this enzyme. We discovered that hexose sugars “turn off” the expression of this gene. So, as long as adequate sugars are available for energy, maintenance, and growth, the production of the mannitolusing enzyme is repressed. After the sugars are gone, mannitol dehydrogenase is produced very rapidly, and this allows mannitol to be used metabolically. This type of gene regulation is ideally designed to help plants cells conserve mannitol as long as possible, which in turn allows the cells to retain stress tolerance as long as possible.

News & Notes: Production, Purification, and Properties of an Endo-1,3-β-Glucanase from the Basidiomycete Agaricus bisporus

1999 ◽  
Vol 38 (3) ◽  
pp. 190-193 ◽  
Author(s):  
Beatriz Galán ◽  
Concepción García Mendoza ◽  
Myriam Calonje ◽  
Monique Novaes-Ledieu
Keyword(s):  
Agaricus Bisporus ◽  
Purification And Properties
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