<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">K. Galanopoulou</style></author><author><style face="normal" font="default" size="100%">C. Scazzochio</style></author><author><style face="normal" font="default" size="100%">M.E. Galinou</style></author><author><style face="normal" font="default" size="100%">W. Liu</style></author><author><style face="normal" font="default" size="100%">F. Borbolis</style></author><author><style face="normal" font="default" size="100%">M. Karachaliou</style></author><author><style face="normal" font="default" size="100%">N. Oestreicher</style></author><author><style face="normal" font="default" size="100%">D.G. Hatzinikolaou</style></author><author><style face="normal" font="default" size="100%">G. Diallinas</style></author><author><style face="normal" font="default" size="100%">S. Amillis</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Purine utilization proteins in the Eurotiales: Cellular compartmentalization, phylogenetic conservation and divergence</style></title><secondary-title><style face="normal" font="default" size="100%">Fungal Genetics and Biology</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2014</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.sciencedirect.com/science/article/pii/S108718451400108X</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">69</style></volume><pages><style face="normal" font="default" size="100%">96-108</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The purine utilization pathway has been thoroughly characterized in &lt;em&gt;Aspergillus nidulans&lt;/em&gt;. We establish&amp;nbsp;here the subcellular distribution of seven key intracellular enzymes, xanthine dehydrogenase (HxA),&amp;nbsp;urate oxidase (UaZ), 5-hydroxy-isourate hydrolase (UaX), 2-oxo-4-hydroxy-4-carboxy ureido imidazoline&amp;nbsp;decarboxylase (UaW), allantoinase (AlX), allantoicase (AaX), ureidoglycolate lyase (UglA), and the fungal specific&amp;nbsp;a-ketoglutarate Fe(II)-dependent dioxygenase (XanA). HxA, AlX, AaX, UaW and XanA are&amp;nbsp;cytosolic, while UaZ, UaX and UglA are peroxisomal. Peroxisomal localization was confirmed by using&amp;nbsp;appropriate pex mutants. The pathway is largely, but not completely conserved in the Eurotiomycetes,&amp;nbsp;noticeably in some species AaX is substituted by an alternative enzyme of probable bacterial origin.&amp;nbsp;UaZ and the urate–xanthine UapA and UapC transporters, are also localized in specific cells of the conidiophore.&amp;nbsp;We show that metabolic accumulation of uric acid occurring in uaZ null mutations is associated&amp;nbsp;with an increased frequency of appearance of morphologically distinct colony sectors, diminished&amp;nbsp;conidiospore production, UV resistance and an altered response to oxidation stress, which may provide&amp;nbsp;a rationale for the conidiophore-specific localization. The pathway-specific transcription factor UaY is&amp;nbsp;localized in both the cytoplasm and nuclei under non-inducing conditions, but it rapidly accumulates&amp;nbsp;exclusively to the nuclei upon induction by uric acid.&lt;/p&gt;</style></abstract></record></records></xml>