Book of Abstracts (PDF) - International Mycological Association
Book of Abstracts (PDF) - International Mycological Association
Book of Abstracts (PDF) - International Mycological Association
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IMC7 Main Congress Theme V: CELL BIOLOGY AND PHYSIOLOGY Posters<br />
produce lolines under certain culture conditions, and a<br />
culture system was developed for regulated loline<br />
expression in this fungus. With this system, genes<br />
differentially expressed during loline accumulation were<br />
isolated by subtractive hybridization. Two genes isolated,<br />
lolA and lolC, were similar to genes encoding aspartate<br />
kinases and homocysteine synthase, respectively, which are<br />
enzymes in methionine biosynthesis. lolA and lolC were<br />
highly expressed during loline production in culture, and<br />
the two genes were present only in endophytes with lolineproducing<br />
phenotypes. Close linkage <strong>of</strong> lolA and lolC in N.<br />
uncinatum was found by PCR, corroborated by data from a<br />
genomic library survey <strong>of</strong> the closely related endophyte E.<br />
festucae. At least five putative genes were found clustered<br />
with lolA and lolC. These putative genes have similarity to<br />
polyamine biosynthesis/interconversion genes, and genes<br />
for monooxygenases, oxidoreductases, demethylases and<br />
aminotransferases, which are frequently found in<br />
secondary-metabolite gene clusters.<br />
1183 - Vacuolar and non-vacuolar protein degradation<br />
routes in the white-rot fungus Phlebia radiata: their<br />
influence on ligninolytic enzymes<br />
M. Staszczak 1 , I. Glina 2 , A. Leonowicz 1 & K.<br />
Grzywnowicz 1*<br />
1 Department <strong>of</strong> Biochemistry, Maria Curie-Sklodowska<br />
University, Pl. M.Curie- Sklodowskiej 3, 20-031 Lublin,<br />
Poland. - 2 Department <strong>of</strong> Cell Biology, Maria Curie-<br />
Sklodowska University, ul. Akademicka 19, 20-033 Lublin,<br />
Poland. - E-mail: grzyw@hermes.umcs.lublin.pl<br />
Continuous protein turnover is involved in basic cellular<br />
functions such as the modulation <strong>of</strong> the levels <strong>of</strong> proteins,<br />
adjustment to stress, as well as preferential removal <strong>of</strong><br />
defective proteins. Eukaryotic cells contain two major<br />
systems for protein degradation: lysosomal (vacuolar) and<br />
non-lysosomal (non-vacuolar). The lysosome was long<br />
believed to be the only site for protein breakdown in cells,<br />
but it is now clear that intracellular proteolysis is largely<br />
accomplished by a highly selective non-lysosomal pathway<br />
that requires a large multicatalytic proteinase complex<br />
known as the proteasome. The 26S eukaryotic proteasome<br />
catalyses the ATP-dependent degradation <strong>of</strong><br />
polyubiquitinated proteins. Lignin-modifying enzymes <strong>of</strong><br />
white-rot fungi are mainly expressed during the secondary<br />
phase <strong>of</strong> growth (idiophase), when the limitation <strong>of</strong> carbon<br />
and nitrogen occurs. It has been demonstrated for many<br />
eukaryotic organisms, that both the vacuolar and nonvacuolar<br />
proteolytic systems are activated by nutrient<br />
starvation. A major goal <strong>of</strong> the present study was to<br />
examine whether the specific agent (CbzLLLal, MG 132)<br />
that blocks the function <strong>of</strong> yeast and mammalian 26S<br />
proteasome and the lysosomotropic agent inhibiting<br />
intralysosomal degradation <strong>of</strong> proteins (chloroquine) can<br />
affect the levels <strong>of</strong> ligninolytic enzymes <strong>of</strong> the white-rot<br />
fungus Phlebia radiata during the shift to idiophase<br />
triggered by nitrogen or carbon starvation. Supported by<br />
the EC Contract ICA2-CT-2000-10050, 5PR-UE/DZ<br />
280/2000.<br />
1184 - Degradation <strong>of</strong> natural and artificial humic acids<br />
by the litter-decomposing basidiomycete Collybia<br />
dryophila<br />
K.T. Steffen 1* , M. H<strong>of</strong>richter 1 & A. Hatakka 2<br />
1 Department <strong>of</strong> Applied Chemistry and Microbiology,<br />
P.O.Box 56, Viikinkaari 9, Bicenter 1, FIN-00014<br />
University <strong>of</strong> Helsinki, Finland. - 2 Dep. <strong>of</strong> Environmental<br />
Biotechnology, <strong>International</strong> Graduate School Zittau,<br />
Markt 23, D-02763 Zittau, Germany. - E-mail:<br />
Kari.Steffen@Helsinki.Fi<br />
The litter decomposing fungus Collybia dryophila is a<br />
common basidiomycete colonizing different types <strong>of</strong> forest<br />
soils. It decomposed in our experiments a natural humic<br />
acid isolated from pine-forest litter (LHA) and a synthetic<br />
14 C-labeled humic acid ( 14 C-HA) prepared from [UL-<br />
14 C]catechol in liquid culture. Polar, lower-molecular mass<br />
fulvic acid (FA) and carbon dioxide were formed during<br />
the degradation. Manganese (200 µn; M Mn 2+ ) enhanced<br />
considerably the decomposition <strong>of</strong> HA leading to 75%<br />
conversion <strong>of</strong> LHA and 50% mineralization <strong>of</strong> 14 C-HA<br />
compared to 60% and 20%, respectively, in the absence <strong>of</strong><br />
Mn 2+ . These findings strongly indicated an involvement <strong>of</strong><br />
the ligninolytic enzyme manganese peroxidase (MnP), the<br />
production <strong>of</strong> which was noticeably increased in Mn 2+ -<br />
supplemented cultures and which was found to be capable<br />
<strong>of</strong> converting LHA in vitro. The enzyme was produced as a<br />
single protein with a pI <strong>of</strong> 4.7 and a molecular weight <strong>of</strong> 44<br />
kDa. In solid-state culture (pine-forest litter), C. dryophila<br />
mineralized 14 C-HA as well and released substantial<br />
amounts <strong>of</strong> water-soluble FA from the insoluble litter<br />
material. The results indicate that litter-decomposing<br />
basidiomycetes such as C. dryophila are involved in humus<br />
turnover by recycling high-molecular mass humic<br />
substances.<br />
1185 - Ultrastructural analysis <strong>of</strong> sterile elements <strong>of</strong><br />
basidiomes and fruitbodies in holobasidiomycetes<br />
A.A. Stepanova<br />
National Institute <strong>of</strong> Desert, Flora and Fauna Ministry <strong>of</strong><br />
Nature Protection Of Turkmenistan,<br />
Ashgabad,744000,Bitarap Turkmenistana,15,<br />
Turkmenistan. - E-mail: iccnet@onlinee.tm<br />
Comparative ultrastructural analysis <strong>of</strong> morphogenesis <strong>of</strong><br />
sterile elements <strong>of</strong> basidiomes (B) in 6 species <strong>of</strong> the<br />
Aphyllophorales and fruitbodies in 17 <strong>of</strong> Agaricales and 1<br />
Gasteromycetes showed that the most specialised are the<br />
cells <strong>of</strong> subhymenium, having the features <strong>of</strong> meristematic<br />
cells. During the grows <strong>of</strong> B and FB the cells <strong>of</strong> sterile<br />
elements are vacuolised, reserve substances, accumulated<br />
in many species, disappear, cytosol and number <strong>of</strong><br />
organelles are reduced.For all studied species (expect the<br />
species <strong>of</strong> Coprinaceae) cells <strong>of</strong> sterile elements has<br />
ultrasructure indicated <strong>of</strong> low level <strong>of</strong> its metabolism. It<br />
was shown, that mass senescence and death <strong>of</strong> the cells <strong>of</strong><br />
<strong>Book</strong> <strong>of</strong> <strong>Abstracts</strong> 359