Phosphoglycerate dehydrogenase is required for kernel development and defines a predominant serine synthesis pathway in maize.

ABSTRACT: Serine functions as both a substrate for protein biosynthesis and a signaling molecule for growth and development. However, the mechanism remains poorly understood. Here, we cloned and functionally characterized the maize (Zea mays) gene Dek20, which encodes phosphoglycerate dehydrogenase1 (PGDH1), the rate-limiting enzyme in the phosphorylated pathway of serine biosynthesis (PPSB). The dek20(Ser282Leu) mutation disrupts the interaction between residues Ser282 and His284, leading to the release of His284, which subsequently binds NAD+/NADH to inhibit serine biosynthesis. Consequently, serine content decreases dramatically, and the cellular response to nutrient starvation is enriched in transcriptome analysis. Serine deficiency triggers tRNASer degradation and reduced translation elongation

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC12164754 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature