<?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%">Sonawane, Prashant D.</style></author><author><style face="normal" font="default" size="100%">Jozawiak, Adam</style></author><author><style face="normal" font="default" size="100%">Barbole, Ranjit</style></author><author><style face="normal" font="default" size="100%">Panda, Sayantan</style></author><author><style face="normal" font="default" size="100%">Abebie, Bekele</style></author><author><style face="normal" font="default" size="100%">Kazachkova, Yana</style></author><author><style face="normal" font="default" size="100%">Gharat, Sachin A.</style></author><author><style face="normal" font="default" size="100%">Ramot, Ofir</style></author><author><style face="normal" font="default" size="100%">Unger, Tamar</style></author><author><style face="normal" font="default" size="100%">Wizler, Guy</style></author><author><style face="normal" font="default" size="100%">Meir, Sagit</style></author><author><style face="normal" font="default" size="100%">Rogachev, Ilana</style></author><author><style face="normal" font="default" size="100%">Doron-Faigenboim, Adi</style></author><author><style face="normal" font="default" size="100%">Petreikov, Marina</style></author><author><style face="normal" font="default" size="100%">Schaffer, Arthur</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author><author><style face="normal" font="default" size="100%">Scherf, Tali</style></author><author><style face="normal" font="default" size="100%">Aharoni, Asaph</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">2-oxoglutarate-dependent dioxygenases drive expansion of steroidal alkaloid structural diversity in the genus Solanum</style></title><secondary-title><style face="normal" font="default" size="100%">New Phytologist</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Solanum</style></keyword><keyword><style  face="normal" font="default" size="100%">specialized metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">steroidal glycoalkaloids (SGAs)</style></keyword><keyword><style  face="normal" font="default" size="100%">structural diversity</style></keyword><keyword><style  face="normal" font="default" size="100%">Tomato</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">234</style></volume><pages><style face="normal" font="default" size="100%">1394-1410</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Solanum steroidal glycoalkaloids (SGAs) are renowned defence metabolites exhibiting spectacular structural diversity. Genes and enzymes generating the SGA precursor pathway, SGA scaffold and glycosylated forms have been largely identified. Yet, the majority of downstream metabolic steps creating the vast repertoire of SGAs remain untapped. Here, we discovered that members of the 2-OXOGLUTARATE-DEPENDENT DIOXYGENASE (2-ODD) family play a prominent role in SGA metabolism, carrying out three distinct backbone-modifying oxidative steps in addition to the three formerly reported pathway reactions. The GLYCOALKALOID METABOLISM34 (GAME34) enzyme catalyses the conversion of core SGAs to habrochaitosides in wild tomato S. habrochaites. Cultivated tomato plants overexpressing GAME34 ectopically accumulate habrochaitosides. These habrochaitoside enriched plants extracts potently inhibit Puccinia spp. spore germination, a significant Solanaceae crops fungal pathogen. Another 2-ODD enzyme, GAME33, acts as a desaturase (via hydroxylation and E/F ring rearrangement) forming unique, yet unreported SGAs. Conversion of bitter alpha-tomatine to ripe fruit, nonbitter SGAs (e.g. esculeoside A) requires two hydroxylations; while the known GAME31 2-ODD enzyme catalyses hydroxytomatine formation, we find that GAME40 catalyses the penultimate step in the pathway and generates acetoxy-hydroxytomatine towards esculeosides accumulation. Our results highlight the significant contribution of 2-ODD enzymes to the remarkable structural diversity found in plant steroidal specialized metabolism.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	10.323&lt;/p&gt;
</style></custom4></record><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%">Lucier, Rosalind</style></author><author><style face="normal" font="default" size="100%">Kamileen, Mohamed O.</style></author><author><style face="normal" font="default" size="100%">Nakamura, Yoko</style></author><author><style face="normal" font="default" size="100%">Serediuk, Sofiia</style></author><author><style face="normal" font="default" size="100%">Barbole, Ranjit</style></author><author><style face="normal" font="default" size="100%">Wurlitzer, Jens</style></author><author><style face="normal" font="default" size="100%">Kunert, Maritta</style></author><author><style face="normal" font="default" size="100%">Heinicke, Sarah</style></author><author><style face="normal" font="default" size="100%">O'Connor, Sarah E.</style></author><author><style face="normal" font="default" size="100%">Sonawane, Prashant D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Steroidal scaffold decorations in Solanum alkaloid biosynthesis</style></title><secondary-title><style face="normal" font="default" size="100%">Molecular Plant</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">a-solamargine</style></keyword><keyword><style  face="normal" font="default" size="100%">Biosynthetic pathway</style></keyword><keyword><style  face="normal" font="default" size="100%">malonyl-solamargine</style></keyword><keyword><style  face="normal" font="default" size="100%">Solanum</style></keyword><keyword><style  face="normal" font="default" size="100%">Specialized metabolites</style></keyword><keyword><style  face="normal" font="default" size="100%">steroidal glycoalkaloids</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2024</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">17</style></volume><pages><style face="normal" font="default" size="100%">1236-1254</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Steroidal glycoalkaloids (SGAs) are specialized metabolites produced by hundreds of Solanum species, including important vegetable crops such as tomato, potato, and eggplant. Although it has been known that SGAs play important roles in defense in plants and ``anti-nutritional''effects (e.g., toxicity and bitterness) to humans, many of these molecules have documented anti-cancer, anti-microbial, antiinflammatory, anti-viral, and anti-pyretic activities. Among these, a-solasonine and a-solamargine isolated from black nightshade (Solanum nigrum) are reported to have potent anti-tumor, anti-proliferative, and anti-inflammatory activities. Notably, a-solasonine and a-solamargine, along with the core steroidal aglycone solasodine, are the most widespread SGAs produced among the Solanum plants. However, it is still unknown how plants synthesize these bioactive steroidal molecules. Through comparative metabolomictranscriptome-guided approach, biosynthetic logic, combinatorial expression in Nicotiana benthamiana, and functional recombinant enzyme assays, here we report the discovery of 12 enzymes from S. nigrum that converts the starting cholesterol precursor to solasodine aglycone, and the downstream a-solasonine, a-solamargine, and malonyl-solamargine SGA products. We further identified six enzymes from cultivated eggplant that catalyze the production of a-solasonine, a-solamargine, and malonyl-solamargine SGAs from solasodine aglycone via glycosylation and atypical malonylation decorations. Our work provides the gene tool box and platform for engineering the production of high-value, steroidal bioactive molecules in heterologous hosts using synthetic biology.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	27.5&lt;/p&gt;
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