GUN4-Porphyrin Complexes Bind the CNH/GUN5 Subunit of Mg-Chelatase and Promote Chlorophyll Biosynthesis in Arabidopsis

Publication Type:Journal Article
Year of Publication:2011
Authors:Adhikari, ND, Froehlich, JE, Strand, DD, Buck, SM, Kramer, DM, Larkin, RM
Journal:The Plant Cell
Volume:23
Issue:4
Date Published:2011
ISBN Number:10404651
Abstract:

The GENOMES UNCOUPLED4 (GUN4) protein stimulates chlorophyll biosynthesis by activating Mg-chelatase, the enzyme that commits protoporphyrin IX to chlorophyll biosynthesis. This stimulation depends on GUN4 binding the ChlH subunit of Mg-chelatase and the porphyrin substrate and product of Mg-chelatase. After binding porphyrins, GUN4 associates more stably with chloroplast membranes and was proposed to promote interactions between ChlH and chloroplast membranes— the site of Mg-chelatase activity. GUN4 was also proposed to attenuate the production of reactive oxygen species (ROS) by binding and shielding light-exposed porphyrins from collisions with O₂ . To test these proposals, we first engineered Arabidopsis thaiiana plants that express only porphyrin binding-deficient forms of GUN4. Using these transgenic plants and particular mutants, we found that the porphyrin binding activity of GUN4 and Mg-chelatase contribute to the accumulation of chlorophyll, GUN4, and Mg-chelatase subunits. Also, we found that the porphyrin binding activity of GUN4 and Mgchelatase affect the associations of GUN4 and ChlH with chloroplast membranes and have various effects on the expression of ROS-inducible genes. Based on our findings, we conclude that ChlH and GUN4 use distinct mechanisms to associate with chloroplast membranes and that mutant alíeles of GUN4 and Mg-chelatase genes cause sensitivity to intense light by a mechanism that is potentially complex.

URL:http://www.jstor.org/stable/41433402
Short Title:The Plant Cell
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