Altered Metabolism in Knockdown Lines of Two HXXXD/BAHD Acyltransferases During Wound Healing in Potato Tubers
2024
Jessica L. Sinka | Indira Queralta-Castillo | Lorena S. Yeung | Isabel Molina | Sangeeta Dhaubhadel | Mark A. Bernards
Suberin biosynthesis involves the coordinated regulation of both phenolic and aliphatic metabolisms. HXXXD/BAHD acyltransferases occupy a unique place in suberization, as they function to crosslink phenolic and aliphatic monomers during suberin assembly. To date, only one suberin-associated HXXXD/BAHD acyltransferase, StFHT, has been described in potatoes, whereas, in Arabidopsis, at least two are implicated in suberin biosynthesis. RNAseq data from wound-induced potato tubers undergoing suberization indicate that transcripts for 28 HXXXD/BAHD acyltransferase genes accumulate in response to wounding. In the present study, we generated RNAi knockdown lines for StFHT and another highly wound-induced HXXXD/BAHD acyltransferase, designated StHCT, and characterized their wound-induced suberin phenotype. StFHT-RNAi and StHCT-RNAi knockdown lines share the same aliphatic suberin phenotype of reduced esterified ferulic acid and ferulates, which is similar to the previously described StFHT-RNAi knockdown suberin phenotype. However, the phenolic suberin phenotype differed between the two knockdown genotypes, with StHCT-RNAi knockdown lines having proportionately more p-hydroxyphenyl-derived moieties than either StFHT-RNAi knockdown or empty vector control lines. Analysis of soluble polar metabolites revealed that StHCT catalyzes a step upstream from StFHT. Overall, our data support the involvement of more than one HXXXD/BAHD acyltransferase in potato suberin biosynthesis.
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