Chlorophyllide a Oxygenase mRNA and Protein Levels Correlate with the Chlorophyll a/b Ratio in Arabidopsis thaliana.
Plants can change the size of their light harvesting complexes in response to growth at different light intensities. Although these changes are small compared to those observed in algae, their conservation in many plant species suggest they play an important role in photoacclimation. A polyclonal antibody to the C-terminus of the Arabidopsis thaliana chlorophyllide a oxygenase (CAO) protein was used to determine if CAO protein levels change under three conditions which perturb chlorophyll levels. These conditions were: (1) transfer to shaded light intensity; (2) limited chlorophyll synthesis, and (3) during photoinhibition. Transfer of wild-type plants from moderate to shaded light intensity resulted in a slight reduction in the Chl a/b ratio, and increases in both CAO and Lhcb1 mRNA levels as well as CAO protein levels. CAO protein levels were also measured in the cch1 mutant, a P642L missense mutation in the H subunit of Mg-chelatase. This mutant has reduced total Chl levels and an increased Chl a/b ratio when transferred to moderate light intensity. After transfer to moderate light intensity, CAO mRNA levels decreased in the cch1 mutant, and a concomitant decrease in CAO protein levels was also observed. Measurements of tetrapyrrole intermediates suggested that decreased Chl synthesis in the cch1 mutant was not a result of increased feedback inhibition at higher light intensity. When wild-type plants were exposed to photoinhibitory light intensity for 3 h, total Chl levels decreased and both CAO mRNA and CAO protein levels were also reduced. These results indicate that CAO protein levels correlate with CAO mRNA levels, and suggest that changes in Chl b levels in vascular plants, are regulated, in part, at the CAO mRNA level.
Harper
Andrea L
AL
Department of Biological Sciences, California State University, Long Beach, 1250 Bellflower Blvd, Long Beach, CA, 90840-3702, USA.|Department of Biochemistry, University of Washington, 1959 NE Pacific St., Seattle, WA, 98195-7350, USA.
von Gesjen
Sigrid E
SE
Department of Biological Sciences, California State University, Long Beach, 1250 Bellflower Blvd, Long Beach, CA, 90840-3702, USA.
Linford
Alicia S
AS
Department of Biological Sciences, California State University, Long Beach, 1250 Bellflower Blvd, Long Beach, CA, 90840-3702, USA.|Department of Biochemistry, University of Washington, 1959 NE Pacific St., Seattle, WA, 98195-7350, USA.
Peterson
Michael P
MP
Department of Biological Sciences, California State University, Long Beach, 1250 Bellflower Blvd, Long Beach, CA, 90840-3702, USA.|Nichols Institute Diagnostics, 1311 Calle Batido, San Clemente, CA, 92673, USA.
Faircloth
Ruth S
RS
Department of Biological Sciences, California State University, Long Beach, 1250 Bellflower Blvd, Long Beach, CA, 90840-3702, USA.|F. Edward Hébert School of Medicine, Uniformed Services University, 4301 Jones Bridge Road, Bethesda, MD, 20814-4799, USA.
Thissen
Michelle M
MM
Department of Biological Sciences, California State University, Long Beach, 1250 Bellflower Blvd, Long Beach, CA, 90840-3702, USA.
Brusslan
Judy A
JA
Department of Biological Sciences, California State University, Long Beach, 1250 Bellflower Blvd, Long Beach, CA, 90840-3702, USA.