A bimodular oxidoreductase mediates the specific reduction of phylloquinone (vitamin K₁) in chloroplasts

The Plant Journal : for Cell and Molecular Biology
Fabienne FurtGilles J C Basset

Abstract

Plants and certain species of cyanobacteria are the only organisms capable of synthesizing phylloquinone (vitamin K₁ for vertebrates), which they use as an electron carrier during photosynthesis. Recent studies, however, have identified a plastidial pool of non-photoactive phylloquinone that could be involved in additional cellular functions. Here, we characterized an Arabidopsis bimodular enzyme--the At4g35760 gene product--comprising an integral domain homologous to the catalytic subunit of mammalian vitamin K₁ epoxide reductase (VKORC1, EC 1.1.4.1) that is fused to a soluble thioredoxin-like moiety. GFP-fusion experiments in tobacco mesophyll cells established that the plant protein is targeted to plastids, and analyses of transcript and protein levels showed that expression is maximal in leaf tissues. The fused and individual VKORC1 domains were separately expressed in yeast, removing their chloroplast targeting pre-sequence and adding a C-terminal consensus signal for retention in the endoplasmic reticulum. The corresponding microsomal preparations were equally effective at mediating the dithiotreitol-dependent reduction of phylloquinone and menaquinone into their respective quinol forms. Strikingly, unlike mammalian VKORC...Continue Reading

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Citations

Oct 24, 2012·Protoplasma·Isabel Aller, Andreas J Meyer
Mar 1, 2012·The Plant Cell·Teresa B FitzpatrickAlisdair R Fernie
Sep 1, 2012·Annual Review of Genetics·Norbert RollandDaphné Seigneurin-Berny
Nov 5, 2013·International Journal of Cell Biology·Yayoi Onda
Jan 17, 2015·International Journal of Molecular Sciences·Nitin A PatilMohammed Akhter Hossain
Aug 13, 2015·Nutrients·Johannes OldenburgCarville G Bevans
Sep 20, 2018·The New Phytologist·Andreas J MeyerNicolas Rouhier

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