Dibin Baby, Sarah Weldi, Marie Knopf, Vinitha Venkadasamy, Jessica Lee Erickson, Petra Bauer
Iron (Fe) homeostasis is regulated to prevent iron imbalance, with the help of redundant basic helix-loop-helix (bHLH) IVc transcription factors that can be controlled by Fe-binding E3 ligases such as BRUTUS (BTS) in Arabidopsis thaliana. However, knowledge gaps remain to fully explain the mechanistic basis of this redundant protein interaction module. The C-terminus of bHLH104 is known to interact with BTS, and structural predictions implicate the three terminal amino acids, proline-alanine-alanine (PAA). However, the importance of the PAA sequence for post-translational regulation of bHLH104 and for the resulting plant phenotypes has not been tested experimentally. Here we show that transgenic plants expressing a bHLH104 variant lacking PAA (b104^dPAA) constitutively upregulate Fe acquisition and Fe transport genes and accumulate Fe, whereas plants expressing wild-type bHLH104 do not. The extent of Fe accumulation in independent b104^dPAA lines correlated positively with b104^dPAA protein abundance. Unlike the wild-type form, b104^dPAA showed no indication of interaction with BTS or of ubiquitination by it. Together, these findings support a model in which the PAA sequence serves as a recognition motif for binding to BTS and for subsequent post-translational regulation of bHLH104. Hence, targeted manipulation of the bHLH IVc protein PAA sequence may represent a strategy for crop biofortification.