2023
DOI: 10.1111/tpj.16354
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The MADS‐box protein SlTAGL1 regulates a ripening‐associated SlDQD/SDH2 involved in flavonoid biosynthesis and resistance against Botrytis cinerea in post‐harvest tomato fruit

Abstract: SUMMARY3‐Dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH) is a key rate‐limiting enzyme that catalyzes the synthesis of the shikimate, which is an important metabolic intermediate in plants and animals. However, the function of SlDQD/SDH family genes in tomato (Solanum lycopersicum) fruit metabolites is still unknown. In the present study, we identified a ripening‐associated SlDQD/SDH member, SlDQD/SDH2, that plays a key role in shikimate and flavonoid metabolism. Overexpression of this gene result… Show more

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Cited by 6 publications
(2 citation statements)
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“…In addition to the reported major proteins, other proteins also play a role in the resistance of B. cinerea. Tomato SlDQD/SDH2 plays a key role in flavonoid biosynthesis and fruit resistance to B. cinerea [119]. Strawberry MANNOSE-BINDING LECTIN 1 (MBL1) is a member of the G-type lectin family and was involved in plant defense against B. cinerea [120].…”
Section: Other Proteinsmentioning
confidence: 99%
“…In addition to the reported major proteins, other proteins also play a role in the resistance of B. cinerea. Tomato SlDQD/SDH2 plays a key role in flavonoid biosynthesis and fruit resistance to B. cinerea [119]. Strawberry MANNOSE-BINDING LECTIN 1 (MBL1) is a member of the G-type lectin family and was involved in plant defense against B. cinerea [120].…”
Section: Other Proteinsmentioning
confidence: 99%
“…Tomato fruit is rich in primary metabolites like sucrose [9][10][11][12], hexoses [13][14][15], organic acids [16][17][18][19][20][21][22][23], and amino acids [24]. Tomato fruit also contains various secondary metabolites, including pigments, mostly lycopene [25][26][27] and beta-carotene [28,29], and antioxidants, namely flavonoids [30][31][32][33][34], and ascorbic acid [35][36][37][38].…”
Section: Introductionmentioning
confidence: 99%