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First published online January 28, 2009; 10.1104/pp.109.135277

Plant Physiology 150:157-166 (2009)
© 2009 American Society of Plant Biologists

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DEVELOPMENT AND HORMONE ACTION

The Barley Magnesium Chelatase 150-kD Subunit Is Not an Abscisic Acid Receptor1,[OA]

André H. Müller and Mats Hansson*

Carlsberg Laboratory, DK–2500 Valby, Copenhagen, Denmark

Magnesium chelatase is the first unique enzyme of the chlorophyll biosynthetic pathway. It is composed of three gene products of which the largest is 150 kD. This protein was recently identified as an abscisic acid receptor in Arabidopsis (Arabidopsis thaliana). We have evaluated whether the barley (Hordeum vulgare) magnesium chelatase large subunit, XanF, could be a receptor for the phytohormone. The study involved analysis of recombinant magnesium chelatase protein as well as several induced chlorophyll-deficient magnesium chelatase mutants with defects identified at the gene and protein levels. Abscisic acid had no effect on magnesium chelatase activity and binding to the barley 150-kD protein could not be shown. Magnesium chelatase mutants showed a wild-type response in respect to postgermination growth and stomatal aperture. Our results question the function of the large magnesium chelatase subunit as an abscisic acid receptor.

1 This work was supported by the Danish Natural Science Research Council.

The author responsible for the distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Mats Hansson (mats{at}crc.dk).

[OA] Open access articles can be viewed online without a subscription.

www.plantphysiol.org/cgi/doi/10.1104/pp.109.135277

* Corresponding author; e-mail mats{at}crc.dk.

Received January 7, 2009; accepted January 22, 2009; published January 28, 2009.


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