Modification of aggregation-prone regions of Arabidopsis glutamyl-tRNA reductase leads to increased stability while maintaining enzyme activity.

ABSTRACT: The aggregation-prone region (APR) is a hydrophobic polypeptide motif that promotes protein aggregation, most commonly in the unfolded or misfolded state. It has been described that chaperones can shield the APRs of proteins, thereby preventing aggregate formation during de novo protein synthesis and stress response. Glutamyl-tRNA reductase (GluTR) is a key enzyme in tetrapyrrole biosynthesis (TBS) which catalyzes the rate-limiting step of 5-aminolevulinic acid synthesis. The GluTR sequence contains two APRs located at the N-terminus, which are suggested to be associated with the dysregulation of protein homeostasis during folding and refolding processes or under stress conditions. It remains open if these APRs directly contribute to GluTR aggregation in vivo, and how their r

SUBMITTER: Ji S 

PROVIDER: S-EPMC11969407 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature