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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chen, Hsien-Jung Huang, Yu-Hsuan Huang, Guan-Jhong Huang, Shyh-Shyun Chow, Te-Jin Lin, Yaw-Huei |
| Description | Author Affiliation: Chen HJ ( Department of Biological Sciences, National Sun Yat-sen University, 804 Kaohsiung, Taiwan. Electronic address: hjchen@faculty.nsysu.edu.tw.); Huang YH ( Department of Biological Sciences, National Sun Yat-sen University, 804 Kaohsiung, Taiwan.); Huang GJ ( Graduate Institute of Chinese Pharmaceutical Sciences, China Medical University, 404 Taichung, Taiwan.); Huang SS ( Graduate Institute of Chinese Pharmaceutical Sciences, China Medical University, 404 Taichung, Taiwan.); Chow TJ ( Department of Biotechnology, Fooyin University, 831 Kaohsiung, Taiwan.); Lin YH ( Institute of Plant and Microbial Biology, Academia Sinica, Nankang, 115 Taipei, Taiwan. Electronic address: boyhlin@gate.sinica.edu.tw.) |
| Abstract | Plant aspartic proteases are generally divided into three categories: typical, nucellin-like, and atypical aspartic proteases based on their gene and protein structures. In this report, a full-length cDNA SPAP1 was cloned from sweet potato leaves, which contained 1515 nucleotides (504 amino acids) and exhibited high amino acid sequence identity (ca. 51-72%) with plant typical aspartic proteases, including tomato LeAspP, potato StAsp, and wheat WAP2. SPAP1 also contained conserved DTG and DSG amino acid residues within its catalytic domain and plant specific insert (PSI) at the C-terminus. The cDNA corresponding to the mature protein (starting from the 66th to 311th amino acid residues) without PSI domain was constructed with pET30a expression vector for fusion protein and antibody production. RT-PCR and protein blot hybridization showed that SPAP1 expression level was the highest in L3 mature leaves, then gradually declined until L5 completely yellow leaves. Ethephon, an ethylene-releasing compound, also enhanced SPAP1 expression at the time much earlier than the onset of leaf senescence. Exogenous application of SPAP1 fusion protein promoted ethephon-induced leaf senescence, which could be abolished by pre-treatment of SPAP1 fusion protein with (a) 95 °C for 5 min, (b) aspartic protease inhibitor pepstatin A, and (c) anti-SPAP1 antibody, respectively. Exogenous SPAP1 fusion protein, whereas, did not significantly affect leaf senescence under dark. These data conclude that sweet potato SPAP1 is a functional typical aspartic protease and participates in ethephon-mediated leaf senescence. The SPAP1-promoted leaf senescence and its activity are likely not associated with the PSI domain. Interaction of ethephon-inducible components for effective SPAP1 promotion on leaf senescence is also suggested. |
| File Format | HTM / HTML |
| ISSN | 01761617 |
| Volume Number | 180 |
| e-ISSN | 16181328 |
| Journal | Journal of Plant Physiology |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-05-15 |
| Publisher Place | Germany |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Botany Aspartic Acid Proteases Metabolism Ipomoea Batatas Enzymology Organophosphorus Compounds Pharmacology Plant Leaves Growth & Development Plant Proteins Amino Acid Sequence Chemistry Base Sequence Darkness Gene Expression Regulation, Plant Drug Effects Hot Temperature Genetics Molecular Sequence Data Phylogeny Recombinant Fusion Proteins Sequence Alignment Time Factors Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology Plant Science Agronomy and Crop Science |
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