תפריט נגישות
ניגודיות עדינהניגודיות גבוהה
מונוכרום
הדגשת קישורים
חסימת אנימציה
פונט קריא
סגור
איפוס הגדרות נגישות
להורדת מודול נגישות חינם תפריט נגישותניגודיות עדינהניגודיות גבוההמונוכרוםהדגשת קישוריםחסימת אנימציהפונט קריאסגוראיפוס הגדרות נגישותלהורדת מודול נגישות חינםAdam Jozwiak - Weizmann Institute of Science, Rehovot, Israel.
Prashant D. Sonawane - Weizmann Institute of Science, Rehovot, Israel
Sayantan Panda- Weizmann Institute of Science, Rehovot, Israel
Hassan Massalha - Weizmann Institute of Science, Rehovot, Israel
Efrat Almekias-Siegl - Weizmann Institute of Science, Rehovot, Israel
Tali Scherf - Weizmann Institute of Science, Rehovot, Israel
Asaph Aharoni - Weizmann Institute of Science, Rehovot, Israel
Sayantan Panda - Agricultural Research Organization—Volcani Center, Rishon LeZion, Israel
Constantine Garagounis - University of Thessaly, Larissa, Greece
Kalliope K. Papadopoulou - University of Thessaly, Larissa, Greece
Glycosylation is one of the most prevalent molecular modifications in nature. Single or multiple sugars can decorate a wide range of acceptors from proteins to lipids, cell wall glycans and small molecules, dramatically affecting their activity. Here, we discovered that by ‘hijacking’ an enzyme of the cellulose synthesis machinery involved in cell wall assembly, plants evolved cellulose synthase-like enzymes (Csls) and acquired the capacity to glucuronidate specialized metabolites, that is, triterpenoid saponins. Apparently, endoplasmic reticulum-membrane localization of Csls and of other pathway proteins was part of evolving a new glycosyltransferase function, as plant metabolite glycosyltransferases typically act in the cytosol. Discovery of glucuronic acid transferases across several plant orders uncovered the long-pursued enzymatic reaction in the production of a low-calorie sweetener from licorice roots. Our work opens the way for engineering potent saponins through microbial fermentation and plant-based systems.
Adam Jozwiak - Weizmann Institute of Science, Rehovot, Israel.
Prashant D. Sonawane - Weizmann Institute of Science, Rehovot, Israel
Sayantan Panda- Weizmann Institute of Science, Rehovot, Israel
Hassan Massalha - Weizmann Institute of Science, Rehovot, Israel
Efrat Almekias-Siegl - Weizmann Institute of Science, Rehovot, Israel
Tali Scherf - Weizmann Institute of Science, Rehovot, Israel
Asaph Aharoni - Weizmann Institute of Science, Rehovot, Israel
Sayantan Panda - Agricultural Research Organization—Volcani Center, Rishon LeZion, Israel
Constantine Garagounis - University of Thessaly, Larissa, Greece
Kalliope K. Papadopoulou - University of Thessaly, Larissa, Greece
Glycosylation is one of the most prevalent molecular modifications in nature. Single or multiple sugars can decorate a wide range of acceptors from proteins to lipids, cell wall glycans and small molecules, dramatically affecting their activity. Here, we discovered that by ‘hijacking’ an enzyme of the cellulose synthesis machinery involved in cell wall assembly, plants evolved cellulose synthase-like enzymes (Csls) and acquired the capacity to glucuronidate specialized metabolites, that is, triterpenoid saponins. Apparently, endoplasmic reticulum-membrane localization of Csls and of other pathway proteins was part of evolving a new glycosyltransferase function, as plant metabolite glycosyltransferases typically act in the cytosol. Discovery of glucuronic acid transferases across several plant orders uncovered the long-pursued enzymatic reaction in the production of a low-calorie sweetener from licorice roots. Our work opens the way for engineering potent saponins through microbial fermentation and plant-based systems.
