%0 Journal Article
%T Affiliation of Dihydrolipoyl Dehydrogenase Allozymes in Mycorrhizae of European Forest Trees and Characterization of the Enzyme of the Matt Bolete (<i>Xerocomus pruinatus</i>) and the Bay Bolete (<i>X. badius</i>)
%A Uwe Schirkonyer
%A Gunter M. Rothe
%J Open Journal of Ecology
%P 356-377
%@ 2162-1993
%D 2018
%I Scientific Research Publishing
%R 10.4236/oje.2018.86022
%X Mycorrhizal roots of the deciduous trees European
beech (</span><i><span style=\"font-family:Verdana;font-size:12px;\">Fagus sylvatica</span></i><span style=\"font-family:Verdana;font-size:12px;\"> (L.)) and
Sessile oak (</span><i><span style=\"font-family:Verdana;font-size:12px;\">Quercus petraea</span></i><span style=\"font-family:Verdana;font-size:12px;\"> (MattuschkaLiebl.)) and the conifers Norway spruce (</span><i><span style=\"font-family:Verdana;font-size:12px;\">Picea abies</span></i><span style=\"font-family:Verdana;font-size:12px;\"> (L.) H. Karst.) and European larch (</span><i><span style=\"font-family:Verdana;font-size:12px;\">Larix decidua</span></i><span style=\"font-family:Verdana;font-size:12px;\"> (Mill.)) associated with
the ectomycorrhizal fungi matt bolete (</span><i><span style=\"font-family:Verdana;font-size:12px;\">Xerocomus
pruinatus</span></i><span style=\"font-family:Verdana;font-size:12px;\"> (Fries 1835)) or bay bolete (</span><i><span style=\"font-family:Verdana;font-size:12px;\">X.
badius</span></i><span style=\"font-family:Verdana;font-size:12px;\"> (Fries 1818)) were analysed with respect to the occurrence of
dihydrolipoyl dehydrogenase (EC 1.8.1.4) allozymes. In root tissues of the two
deciduous trees</span></span><span style=\"font-family:Verdana;\">,</span><span style=\"font-size:10pt;font-family:&quot;\"><span style=\"font-family:Verdana;font-size:12px;\"> two gene loci could be
visualized after cellulose acetate electrophoresis while three loci were expressed
in root tissues of the two coniferous species. The two fungal species and
further ectomycorrhizal fungi expressed exclusively one dihydrolipoyl
dehydrogenase gene. In </span><i><span style=\"font-family:Verdana;font-size:12px;\">Xerocomus
pruinatus</span></i><span style=\"font-family:Verdana;font-size:12px;\"> and </span><i><span style=\"font-family:Verdana;font-size:12px;\">X. badius</span></i></span><span style=\"font-family:Verdana;\">,</span><span style=\"font-size:10pt;font-family:&quot;\"><span style=\"font-family:Verdana;font-size:12px;\"> the dihydrolipoyl dehydrogenase gene consists of 1460 bp and 1370 bp,
respectively, including five introns each consisting of 52 bp. Their DNA
sequences correspond to 70 to 90% to other fungal dihydrolipoyl dehydrogenase
genes. One monomer of the dimeric dihydrolipoyl dehydrogenase enzyme consists
of 486 (</span><i><span style=\"font-family:Verdana;font-size:12px;\">X. pruinatus</span></i><span style=\"font-family:Verdana;font-size:12px;\">) or 454 (</span><i><span style=\"font-family:Verdana;font-size:12px;\">X.
%K Amino Acid Sequence
%K cDNA
%K Ectomycorrhizae
%K Fagus sylvatica
%K Gene Sequence
%K &lt
%K i&gt
%K Larix decidua&lt
%K /i&gt
%K mRNA
%K Dihydrolipoyl Dehydrogenase
%K &lt
%K i&gt
%K Picea abies
%K Quercus petraea
%K Xerocomus pruinatus
%K Xerocomus badius&lt
%K /i&gt
%U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=85310