Subcellular evidence for the involvement of peroxisomes in plant isoprenoid biosynthesis

被引：14

作者：

Clastre, Marc ^{[1
]}

Papon, Nicolas ^{[1
]}

Courdavault, Vincent ^{[1
]}

Giglioli-Guivarc'h, Nathalie ^{[1
]}

St-Pierre, Benoit ^{[1
]}

Simkin, Andrew J. ^{[1
]}

机构：

[1] Univ Francois Rabelais Tours, EA2106, Biomol & Biotechnol Vegetales, Tours, France

来源：

PLANT SIGNALING & BEHAVIOR | 2011年 / 6卷 / 12期

关键词：

peroxisome; mevalonic acid; pathway; 5-phosphomevalonate kinase; mevalonate 5-diphosphate decarboxylase; farnesyl diphosphate synthase; isoprenoid; Catharanthus roseus; Arabidopsis thaliana;

D O I：

10.4161/psb.6.12.18173

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：

The role of peroxisomes in isoprenoid metabolism, especially in plants, has been questioned in several reports. A recent study of Sapir-Mir et al.(1) revealed that the two isoforms of isopentenyl diphosphate (IPP) isomerase, catalyzing the isomerization of IPP to dimethylallyl diphosphate (DMAPP) are found in the peroxisome. In this addendum, we provide additional data describing the peroxisomal localization of 5-phosphomevalonate kinase and mevalonate 5-diphosphate decarboxylase, the last two enzymes of the mevalonic acid pathway leading to IPP.(2) This finding was reinforced in our latest report showing that a short isoform of farnesyl diphosphate, using IPP and DMAPP as substrates, is also targeted to the organelle.(3) Therefore, the classical sequestration of isoprenoid biosynthesis between plastids and cytosol/ER can be revisited by including the peroxisome as an additional isoprenoid biosynthetic compartment within plant cells.

引用

页码：2044 / 2046

页数：3

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