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Published on January 28, 2009; 10.1104/pp.109.135277

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Received January 7, 2009
Accepted January 22, 2009

The barley magnesium chelatase 150-kDa subunit is not an abscisic acid receptor

Andre H. Muller and Mats Hansson *

Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Valby, Copenhagen, Denmark

* Corresponding author; email: mats{at}crc.dk.

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 kDa. This protein was recently identified as an abscisic acid receptor in Arabidopsis thaliana (Shen et al., 2006. Nature 443, 823-826). We have evaluated whether the barley (Hordeum vulgare L.) 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 did not bind to the barley 150-kDa protein. Magnesium chelatase mutants showed a wild-type response in respect to post-germination growth and stomatal aperture. Our results question the validity of the idea that the large magnesium chelatase subunit is an abscisic acid receptor.




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