Glutaredoxins regulate maize inflorescence meristem development via redox control of TGA transcriptional activity

Glutaredoxins are small redox proteins that use glutathione as a cofactor. In maize, a glutaredoxin named MSCA1 controls the activity of transcription factor FASCIATED EAR4 through dimerization, regulating inflorescence meristem development. Glutaredoxins (GRXs) are small oxidoreductases that can modify target protein activities through control of the redox (reduction/oxidation) state by reducing or glutathionylating disulfide bridges. Although CC-type GRXs are plant specific and play important roles in many processes, the mechanisms by which they modulate the activity of target proteins in vivo are unknown. In this study, we show that a maize CC-type GRX, MALE STERILE CONVERTED ANTHER1 (MSCA1), acts redundantly with two paralogues, ZmGRX2 and ZmGRX5, to modify the redox state and the activity of its putative target, the TGA transcription factor FASCIATED EAR4 (FEA4) that acts as a negative regulator of inflorescence meristem development. We used CRISPR-Cas9 to create a GRX triple knockout, resulting in severe suppression of meristem, ear and tassel growth and reduced plant height. We further show that GRXs regulate the redox state, DNA accessibility and transcriptional activities of FEA4, which acts downstream of MSCA1 and its paralogues to control inflorescence development. Our findings reveal the function of GRXs in meristem development, and also provide direct evidence for GRX-mediated redox modification of target proteins in plants.

Automated summary

Glutaredoxins are small redox proteins that regulate the activity of transcription factors in maize, controlling inflorescence meristem development. The maize CC-type glutaredoxin MSCA1, along with its paralogues ZmGRX2 and ZmGRX5, modify the redox state and activity of the transcription factor FASCIATED EAR4, ultimately affecting inflorescence development. The study highlights the role of glutaredoxins in meristem development and provides evidence for their redox modification of target proteins in plants.