The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein

@article{Fang2016TheAG,
  title={The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein},
  author={Ying Fang and Shun Zhao and Feilong Zhang and Aiguo Zhao and Wenxia Zhang and M. Zhang and L. Liu},
  journal={Scientific Reports},
  year={2016},
  volume={6}
}
Tetrapyrrole biosynthesis is an essential and tightly regulated process, and glutamyl-tRNA reductase (GluTR) is a key target for multiple regulatory factors at the post-translational level. By binding to the thylakoid membrane protein FLUORESCENT (FLU) or the soluble stromal GluTR-binding protein (GBP), the activity of GluTR is down- or up-regulated. Here, we reconstructed a ternary complex composed of the C-terminal tetratricopepetide-repeat domain of FLU, GBP, and GluTR, crystallized and… Expand
Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis
Fluorescence in blue light (FLU) is involved in inactivation and localization of glutamyl‐tRNA reductase during light exposure
Peanut genes encoding tetrapyrrole biosynthetic enzymes, AhHEMA1 and AhFC1, alleviating the salt stress in transgenic tobacco.
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