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

被引：70

作者：

Meskauskiene, R ^{[1
]}

Apel, K ^{[1
]}

机构：

[1] Swiss Fed Inst Technol, Swiss Fed Inst Technol, Inst Plant Sci, CH-8092 Zurich, Switzerland

来源：

FEBS LETTERS | 2002年 / 532卷 / 1-2期

关键词：

protochlorophyllide; FLU; glutamyl-tRNA reductase; glutamate-1-semialdehyde-2-1-amino transferase; Arabidopsis;

D O I：

10.1016/S0014-5793(02)03617-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 delta-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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：27 / 30

页数：4

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