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PMID:15805480
Citation |
Yamasato, A, Nagata, N, Tanaka, R and Tanaka, A (2005) The N-terminal domain of chlorophyllide a oxygenase confers protein instability in response to chlorophyll B accumulation in Arabidopsis. Plant Cell 17:1585-97 |
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Abstract |
Plants acclimate to variations in light intensity by changing the antenna size of photosystems. This acclimation allows them to undergo efficient photosynthesis and creates a protective strategy to minimize photodamage. Chlorophyll b synthesis by chlorophyllide a oxygenase (CAO) is a key regulatory step in the control of antenna size. Recently, we found that higher plant CAOs consist of three domains (A, B, and C domains) and confirmed that the C domain possesses catalytic function. To investigate the function of the A domain, we fused various combinations of these three domains with green fluorescent protein (GFP) and introduced them into Arabidopsis thaliana. When a full-length CAO-GFP fusion protein was introduced into a chlorophyll b-less chlorina1-1 mutant, chlorophyll b accumulated to almost the same levels as in the chlorophyll b-containing Columbia wild type, but the CAO-GFP could not be detected by immunoblotting. By contrast, when a GFP-C domain fusion was introduced into chlorina1-1 or Columbia wild type, a large amount of GFP-C domain protein accumulated and the chlorophyll a/b ratio decreased drastically from 3.6 to 2.2 in Columbia wild type. When an A domain-GFP was introduced into Columbia wild type, A domain-GFP levels were very low. Conversely, a large amount of the protein accumulated when it was introduced into the chlorina1-1 mutant. These results indicate that the A domain may sense the presence of chlorophyll b and regulate the accumulation of CAO protein in the chloroplasts. |
Links |
PubMed PMC1091776 Online version:10.1105/tpc.105.031518 |
Keywords |
Arabidopsis/genetics; Arabidopsis/metabolism; Chlorophyll/metabolism; Chloroplasts/genetics; Chloroplasts/metabolism; Feedback, Physiological/genetics; Green Fluorescent Proteins/metabolism; Mutation/physiology; Oxygenases/metabolism; Photosynthesis/physiology; Plant Proteins/metabolism; Protein Structure, Tertiary/physiology; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism |
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