Interaction of FLU, a negative regulator of tetrapyrrole biosynthesis, with the glutamyl-tRNA reductase requires the tetratricopeptide repeat domain of FLU
| Autor: | Klaus Apel, Rasa Meskauskiene |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Repetitive Sequences
Amino Acid FLU Glutamate-1-semialdehyde-2-1-amino transferase Biophysics Arabidopsis Reductase Biology Biochemistry chemistry.chemical_compound Biosynthesis Protochlorophyllide Structural Biology Glutamyl-tRNA reductase Two-Hybrid System Techniques Genetics Pyrroles Molecular Biology Heme Intramolecular Transferases chemistry.chemical_classification Coiled coil Arabidopsis Proteins Cell Biology Aldehyde Oxidoreductases Yeast Protein Structure Tertiary Tetratricopeptide Enzyme chemistry Tetrapyrroles |
| Zdroj: | FEBS letters. 532(1-2) |
| ISSN: | 0014-5793 |
| Popis: | Regulation of tetrapyrrole biosynthesis in plants has been attributed to feedback control of glutamyl-tRNA reductase (GLU-TR) by heme. Recently, another negative regulator, the FLU protein, has been discovered that operates independently of heme. A truncated form of FLU that contains two domains implicated in protein–protein interaction was co-expressed in yeast with either GLU-TR or glutamate-1-semialdehyde-2-1-aminotransferase (GSA-AT), the second enzyme involved in δ-aminolevulinic acid (ALA) biosynthesis. FLU interacts strongly with GLU-TR but not with GSA-AT. Two variants of FLU that carry single amino acid exchanges within their coiled coil and tetratricopeptide repeat (TPR) domains, respectively, were also tested. Only the FLU variant with the mutated TPR motif lost the capacity to interact with GLU-TR. |
| Databáze: | OpenAIRE |
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