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Plant and Cell Physiology, 2002, Vol. 43, No. 9 984-991
© 2002 Oxford University Press

Molecular Characterization of a Senescence-Associated Gene Encoding Cysteine Proteinase and its Gene Expression during Leaf Senescence in Sweet Potato

Guan-Hong Chen1, Lin-Tzu Huang2, Mee-Ngan Yap2, Ruey-Hua Lee2, Yih-Jong Huang3, Ming-Chih Cheng2 and Shu-Chen Grace Chen2,1

1 Institute of Biochemistry, School of Life Science, National Yang-Ming University, Taipei, Taiwan
2 Institute of Botany, Academia Sinica, Nankang, Taipei, Taiwan
3 Graduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan
The first two authors contributed equally to this work.

The structure and expression of a senescence-associated gene (SPG31) encoding a cysteine proteinase precursor of sweet potato have been characterized. The coding region of the gene consists of two exons encoding an enzyme precursor of 341 amino acids with conserved catalytic amino acids of papain. Examination of the expression patterns of the SPG31 gene in sweet potato by Northern blot analyses reveals that the transcripts of SPG31 are specifically induced in the senescing leaves but not in other organs. The differential accumulation of the mature SPG31 protein in the senescing leaves was further identified by two-dimensional electrophoresis of leaf proteins and N-terminal sequencing. This result suggests the important role played by SPG31 in proteolysis and nitrogen remobilization during the leaf senescence process. Furthermore, treatment of mature green leaves with ethylene for 3 d resulted in a high-level induction of SPG31 transcripts. Ethylene-regulated expression of SPG31 is consistent with the presence of a number of putative ethylene-responsive elements in the 899-bp SPG31 promoter region.

1 Corresponding author: E-mail, boscchen@ccvax.sinica.edu.tw; Fax, 8862-27827954.


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