<?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%">Itkin, M.</style></author><author><style face="normal" font="default" size="100%">Heinig, U.</style></author><author><style face="normal" font="default" size="100%">Tzfadia, O.</style></author><author><style face="normal" font="default" size="100%">Bhide, Amey J.</style></author><author><style face="normal" font="default" size="100%">Shinde, B.</style></author><author><style face="normal" font="default" size="100%">Cardenas, Pablo D.</style></author><author><style face="normal" font="default" size="100%">Bocobza, S. E.</style></author><author><style face="normal" font="default" size="100%">Unger, T.</style></author><author><style face="normal" font="default" size="100%">Malitsky, Sergey</style></author><author><style face="normal" font="default" size="100%">Finkers, R.</style></author><author><style face="normal" font="default" size="100%">Tikunov, Y.</style></author><author><style face="normal" font="default" size="100%">Bovy, A.</style></author><author><style face="normal" font="default" size="100%">Chikate, Y.</style></author><author><style face="normal" font="default" size="100%">Singh, P.</style></author><author><style face="normal" font="default" size="100%">Rogachev, I.</style></author><author><style face="normal" font="default" size="100%">Beekwilder, J.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</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%">Biosynthesis of antinutritional alkaloids in solanaceous crops is mediated by clustered genes</style></title><secondary-title><style face="normal" font="default" size="100%">Science</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">6142</style></number><publisher><style face="normal" font="default" size="100%">AMER ASSOC ADVANCEMENT SCIENCE</style></publisher><pub-location><style face="normal" font="default" size="100%">1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA</style></pub-location><volume><style face="normal" font="default" size="100%">341</style></volume><pages><style face="normal" font="default" size="100%">175-179</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) such as alpha-solanine found in solanaceous food plants-as, for example, potato-are antinutritional factors for humans. Comparative coexpression analysis between tomato and potato coupled with chemical profiling revealed an array of 10 genes that partake in SGA biosynthesis. We discovered that six of them exist as a cluster on chromosome 7, whereas an additional two are adjacent in a duplicated genomic region on chromosome 12. Following systematic functional analysis, we suggest a revised SGA biosynthetic pathway starting from cholesterol up to the tetrasaccharide moiety linked to the tomato SGA aglycone. Silencing GLYCOALKALOID METABOLISM 4 prevented accumulation of SGAs in potato tubers and tomato fruit. This may provide a means for removal of unsafe, antinutritional substances present in these widely used food crops.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6142</style></issue><custom2><style face="normal" font="default" size="100%">&lt;p&gt;Council of Scientific &amp;amp; Industrial Research (CSIR) - India&lt;/p&gt;</style></custom2><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">31.477
</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%">Sonawane, Prashant D.</style></author><author><style face="normal" font="default" size="100%">Gharat, Sachin A.</style></author><author><style face="normal" font="default" size="100%">Jozwiak, Adam</style></author><author><style face="normal" font="default" size="100%">Barbole, Ranjit</style></author><author><style face="normal" font="default" size="100%">Heinicke, Sarah</style></author><author><style face="normal" font="default" size="100%">Almekias-Siegl, Efrat</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%">O'Connor, Sarah E.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</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%">BAHD-type acyltransferase concludes the biosynthetic pathway of non-bitter glycoalkaloids in ripe tomato fruit</style></title><secondary-title><style face="normal" font="default" size="100%">Nature Communications</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">14</style></volume><pages><style face="normal" font="default" size="100%">4540</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	During tomato fruit ripening, bitter and toxic steroidal glycoalkaloids (SGAs) are converted to nonbitter and less toxic forms, but proposed acylating enzyme in pathway remain unknown. Here, authors report BAHD-type acyltransferase that catalyze acylation step in biosynthesis of non-bitter SGAs in tomato. Tomato is the highest value fruit and vegetable crop worldwide, yet produces &amp;amp; alpha;-tomatine, a renowned toxic and bitter-tasting anti-nutritional steroidal glycoalkaloid (SGA) involved in plant defense. A suite of modifications during tomato fruit maturation and ripening converts &amp;amp; alpha;-tomatine to the non-bitter and less toxic Esculeoside A. This important metabolic shift prevents bitterness and toxicity in ripe tomato fruit. While the enzymes catalyzing glycosylation and hydroxylation reactions in the Esculeoside A pathway have been resolved, the proposed acetylating step remains, to date, elusive. Here, we discovered that GAME36 (GLYCOALKALOID METABOLISM36), a BAHD-type acyltransferase catalyzes SGA-acetylation in cultivated and wild tomatoes. This finding completes the elucidation of the core Esculeoside A biosynthetic pathway in ripe tomato, allowing reconstitution of Esculeoside A production in heterologous microbial and plant hosts. The involvement of GAME36 in bitter SGA detoxification pathway points to a key role in the evolution of sweet-tasting tomato as well as in the domestication and breeding of modern cultivated tomato fruit.&lt;/p&gt;
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	Foreign&lt;/p&gt;
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