Polyploidy and diploidization in soybean

Yuan, Jingya; Song, Qingxin

doi:10.1007/s11032-023-01396-y

Cited by 4 publications

(2 citation statements)

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“…In addition, GmADTs in each subgroup are clustered with ADT sequences with other legume species ( Medicago truncatula, Lotus japonicus , and Phaseolus vulgaris ). As observed for most of the gene families in soybean, GmADTs mostly group in pairs, consistent with its recent whole genome duplication ( Schmutz et al., 2010 ; Yuan and Song, 2023 ). Subgroups II and III contain other plant ADTs that have been shown to act as PDTs (eg.…”

Section: Resultssupporting

confidence: 76%

“…There have been multiple whole genome duplications (WGDs) in the evolutionary history of soybean. Aside from the ancient WGD shared by all angiosperms ( Young and Bharti, 2012 ), soybean has undergone two more recent WGDs: one just prior to radiation of legumes (~58-59 million years ago), and one Glycine -specific WGD that ocurred ~13-14 million years ago ( Shoemaker et al., 2006 ; Schmutz et al., 2010 ; Yuan and Song, 2023 ). As a result, soybean has many duplicated genes, including the GmADT family members.…”

Section: Discussionmentioning

confidence: 99%

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Soybean AROGENATE DEHYDRATASES (GmADTs): involvement in the cytosolic isoflavonoid metabolon or trans-organelle continuity?

Clayton,

Islam,

Pannunzio

et al. 2024

Front. Plant Sci.

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Soybean (Glycine max) produces a class of phenylalanine (Phe) derived specialized metabolites, isoflavonoids. Isoflavonoids are unique to legumes and are involved in defense responses in planta, and they are also necessary for nodule formation with nitrogen-fixing bacteria. Since Phe is a precursor of isoflavonoids, it stands to reason that the synthesis of Phe is coordinated with isoflavonoid production. Two putative AROGENATE DEHYDRATASE (ADT) isoforms were previously co-purified with the soybean isoflavonoid metabolon anchor ISOFLAVONE SYNTHASE2 (GmIFS2), however the GmADT family had not been characterized. Here, we present the identification of the nine member GmADT family. We determined that the GmADTs share sequences required for enzymatic activity and allosteric regulation with other characterized plant ADTs. Furthermore, the GmADTs are differentially expressed, and multiple members have dual substrate specificity, also acting as PREPHENATE DEHYDRATASES. All GmADT isoforms were detected in the stromules of chloroplasts, and they all interact with GmIFS2 in the cytosol. In addition, GmADT12A interacts with multiple other isoflavonoid metabolon members. These data substantiate the involvement of GmADT isoforms in the isoflavonoid metabolon.

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Section: Resultssupporting

confidence: 76%