Interaction of FLU, a negative regulator of tetrapyrrole biosynthesis, with the glutamyl‐tRNA reductase requires the tetratricopeptide repeat domain of FLU

FEBS Letters

Meskauskiene, Rasa¹  Apel, Klaus¹ 

[1] Institute of Plant Sciences, Swiss Federal Institute of Technology (ETH), Universitätstr. 2, 8092 Zürich, Switzerland

关键词: Protochlorophyllide;    FLU;    Glutamyl-tRNA reductase;    Glutamate-1-semialdehyde-2-1-amino transferase;    Arabidopsis;    ALA;    δ-aminolevulinic acid;    Chlide;    chlorophyllide;    GLU-TR;    glutamyl-tRNA reductase;    GSA-AT;    glutamate-1-semialdehyde-2-1-aminotransferase;    Pchlide;    protochlorophyllide;    POR;    NADPH-protochlorophyllide oxidoreductase;    TPR;    tetratricopeptide repeat;   

DOI  :  10.1016/S0014-5793(02)03617-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown