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First published online March 21, 2008; 10.1104/pp.108.118430 Plant Physiology 147:179-187 (2008) © 2008 American Society of Plant Biologists OPEN ACCESS ARTICLE
Amino Acid Substitutions in Homologs of the STAY-GREEN Protein Are Responsible for the green-flesh and chlorophyll retainer Mutations of Tomato and Pepper1,[W],[OA]Department of Horticulture, Michigan State University, East Lansing, Michigan 48824 (C.S.B.); Boyce Thompson Institute for Plant Research, Ithaca, New York 14853 (C.S.B., R.P.M., M.-Y.C., A.B., J.J.G.); and U.S. Department of Agriculture Agricultural Research Service, Plant, Soil and Nutrition Laboratory, Ithaca, New York 14853 (R.P.M., J.J.G.)
Color changes often accompany the onset of ripening, leading to brightly colored fruits that serve as attractants to seed-dispersing organisms. In many fruits, including tomato (Solanum lycopersicum) and pepper (Capsicum annuum), there is a sharp decrease in chlorophyll content and a concomitant increase in the synthesis of carotenoids as a result of the conversion of chloroplasts into chromoplasts. The green-flesh (gf) and chlorophyll retainer (cl) mutations of tomato and pepper, respectively, are inhibited in their ability to degrade chlorophyll during ripening, leading to the production of ripe fruits characterized by both chlorophyll and carotenoid accumulation and are thus brown in color. Using a positional cloning approach, we have identified a point mutation at the gf locus that causes an amino acid substitution in an invariant residue of a tomato homolog of the STAY-GREEN (SGR) protein of rice (Oryza sativa). Similarly, the cl mutation also carries an amino acid substitution at an invariant residue in a pepper homolog of SGR. Both GF and CL expression are highly induced at the onset of fruit ripening, coincident with the ripening-associated decline in chlorophyll. Phylogenetic analysis indicates that there are two distinct groups of SGR proteins in plants. The SGR subfamily is required for chlorophyll degradation and operates through an unknown mechanism. A second subfamily, which we have termed SGR-like, has an as-yet undefined function.
1 This work was supported by Michigan State University and the Michigan Agricultural Experiment Station (grant to C.B.), and National Science Foundation Plant Genome grants (grant nos. 05–01778 and 06–06595 to J.G.). The author responsible for 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: Cornelius S. Barry (barrycs{at}msu.edu). [W] The online version of this article contains Web-only data. [OA] Open Access articles can be viewed online without a subscription. www.plantphysiol.org/cgi/doi/10.1104/pp.108.118430 * Corresponding author; e-mail barrycs{at}msu.edu. Received February 26, 2008; accepted March 17, 2008; published March 21, 2008. This article has been cited by other articles:
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