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Published on April 27, 2007; 10.1104/pp.107.100172


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Received March 25, 2007
Accepted April 13, 2007

Identification of a Novel Chloroplast Protein AtNYE1 Regulating Chlorophyll Degradation during Leaf Senescence in Arabidopsis

Guodong Ren , Kun An , Yang Liao , Xiao Zhou , Yajun Cao , Huifang Zhao , Xiaochun Ge , and Benke Kuai *

State Key Laboratory of Genetic Engineering, Department of Biochemistry, School of Life Sciences, Fudan University, Shanghai 200433, China

* Corresponding author; email: bbkuai{at}fudan.edu.cn.

A dramatic increase of chlorophyll (Chl) degradation occurs during senescence of vegetative plant organs and fruit ripening. Although the biochemical pathway of Chl degradation has long been proposed, little is known about its regulatory mechanism. Identification of Chl degradation-disturbed mutants and subsequently isolation of responsible genes would greatly facilitate the elucidation of the regulation of Chl degradation. Here, we describe a non-yellowing mutant of Arabidopsis, nye1-1, in which 50% Chls was retained, compared to less than 10% in the wild type (Col-0), at the end of a six-day dark incubation. Nevertheless, neither photosynthesis- nor senescence-associated process was significantly affected in nye1-1. Characteristically, a significant reduction in PaO activity was detected in nye1-1. However, no detectable accumulation of either chlorophyllide a or pheophorbide a was observed. Reciprocal crossings revealed that the mutant phenotype was caused by a monogenic semi-dominant nuclear mutation. We have identified AtNYE1 by positional cloning. Dozens of its putative orthologs, predominantly appeared in higher plant species, were identified, some of which have been associated with Chl degradation in a few crop species. qPCR analysis showed that AtNYE1 was drastically induced by senescence signals. Constitutive over-expression of AtNYE1 could result in either pale-yellow true leaves or even albino seedlings. These results collectively indicate that NYE1 plays an important regulatory role in Chl degradation during senescence by modulating PaO activity.




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