Isolation, structure modeling and function characterization of a trypsin inhibitor from Cassia obtusifolia
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- 作者：Zubi Liu (1)
Qiankun Zhu (2)
Juanjuan Li (1)
Gan Zhang (1)
Aerguli Jiamahate (1)
Jiayu Zhou (1)
Hai Liao (1)
1. School of Life Science and Engineering ; Southwest Jiaotong University ; Chengdu ; 610031 ; China
2. College of Life Sciences ; Zhejiang University ; Hangzhou ; 310058 ; China - 关键词：Cassia obtusifolia ; Insectcidal trypsin inhibitor ; Lepidopterous pests ; Molecular cloning ; Molecular modeling ; Trypsin inhibitor ; Trypsin ; like proteases
- 刊名：Biotechnology Letters
- 出版年：2015
- 出版时间：April 2015
- 年：2015
- 卷：37
- 期：4
- 页码：863-869
- 全文大小：948 KB
- 参考文献：1. Bhattacharjee, N, Banerjee, S, Dutta, SK (2014) Cloning, expression and mutational studies of a trypsin inhibitor that retains activity even after cyanogen bromide digestion. Protein Expr Purif 96: pp. 26-31 CrossRef
2. Callis, J (1995) Regulation of protein degradation. Plant Cell 7: pp. 845-857 CrossRef
3. Meester, P, Brick, P, Lloyd, LF, Blow, DM, Onesti, S (1998) Structure of the Kunitz-type soybean trypsin inhibitor (STI): implication for the interactions between members of the STI family and tissue-plasminogen activator. Acta Crystallogr D Biol Crystallogr 54: pp. 589-597 CrossRef
4. Dreon, MS, Ituarte, S, Heras, H (2010) The role of the proteinase inhibitor ovorubin in apple snail eggs resembles plant embryo defense against predation. PLoS One 5: pp. e15059 CrossRef
5. Erlanger, BF, Kokowsky, N, Cohen, W (1961) The preparation and properties of two new chromogenic substrates of trypsin. Arch Biochem Biophys 95: pp. 271-280 CrossRef
6. Kim, SJ, Kim, KW, Kim, DS, Kim, MC, Jeon, YD, Kim, SG, Jung, HJ, Jang, HJ, Lee, BC, Chung, WS, Hong, SH, Chung, SH, Um, JY (2011) The protective effect of Cassia obtusifolia on DSS-induced colitis. Am J Chin Med 39: pp. 565-577 CrossRef
7. Liao, H, Ren, W, Kang, Z, Jiang, JH, Zhao, XJ, Du, LF (2007) A trypsin inhibitor from Cassia obtusifolia seeds: isolation, characterization and activity against Pieris rapae. Biotechnol Lett 29: pp. 653-658 CrossRef
8. Liu, Z, Song, T, Zhu, Q, Wang, W, Zhou, J, Liao, H (2014) De novo assembly and analysis of Cassia obtusifolia seed transcriptome to identify genes involved in the biosynthesis of active metabolites. Biosci Biotechnol Biochem 78: pp. 791-799 CrossRef
9. Nixon, A, Wood, CR (2006) Engineered protein inhibitors of proteases. Curr Opin Drug Discov Dev 9: pp. 261-268
10. Oliveira, AS, Migliolo, L, Aquino, RO, Ribeiro, JK, Macedo, LL, Bemquerer, MP, Santos, EA, Kiyota, S, Sales, MP (2009) Two Kunitz-type inhibitors with activity against trypsin and papain from Pithecellobium dumosum seeds: purification, characterization, and activity towards pest insect digestive enzyme. Protein Pept Lett 16: pp. 1526-1532 CrossRef
11. Rawlings, ND, Tolle, DP, Barrett, AJ (2004) Evolutionary families of peptidase inhibitors. Biochem J 378: pp. 705-716 CrossRef
12. Sali, A (1995) Comparative protein modeling by satisfaction of spatial restraints. Mol Med Today 1: pp. 270-277 CrossRef
13. Sob, SVT, Wabo, HK, Tchinda, AT, Tane, P, Ngadjui, BT, Ye, Y (2010) Anthraquinones, sterols, triterpenoids and xanthones from Cassia obtusifolia. Biochem Syst Ecol 38: pp. 342-345 CrossRef
14. Srinivasan, T, Kumar, KR, Kirti, PB (2009) Constitutive expression of a trypsin protease inhibitor confers multiple stress tolerance in transgenic tobacco. Plant Cell Physiol 50: pp. 541-553 CrossRef
15. Zhou, D, Lobo, YA, Batista, IF, Marques-Porto, R, Gustchina, A, Oliva, ML, Wlodawer, A (2013) Crystal structures of a plant trypsin inhibitor from Enterolobium contortisiliquum (EcTI) and of its complex with bovine trypsin. PLoS One 8: pp. e62252 CrossRef
16. Zhu, Q, Zou, J, Zhu, M, Liu, Z, Feng, P, Fan, G, Wang, W, Liao, H (2014) In silico analysis on structure and DNA binding mode of AtNAC1, a NAC transcription factor from Arabidopsis thaliana. J Mol Model 20: pp. 2117 CrossRef - 刊物类别：Biomedical and Life Sciences
- 刊物主题：Life Sciences
Microbiology
Biotechnology
Applied Microbiology
Biochemistry - 出版者：Springer Netherlands
- ISSN：1573-6776
文摘
A trypsin inhibitor gene (CoTI1) from Cassia obtusifolia was isolated and the deduced amino acid sequence was attributed to the Kunitz-type trypsin inhibitor. The recombined CoTI1, expressed in E. coli, exhibited strong inhibitory effect on bovine trypsin and trypsin-like proteases from Helicoverpa armigera, Spodoptera exigua, and Spodoptera litura. CoTI1 thus presents insecticidal properties that may be useful for the genetic engineering of plants. Leu84, Arg86 and Thr88 were predicted as three key residues by molecular modeling in which Arg86, inserted into the substrate pocket of trypsin, interacted directly with residue Asp189 of trypsin causing the specific inhibition against trypsin. The predicted results were confirmed by site-directed mutagenesis with L84A, R86A and T88A, respectively. The substantial changing expression level of CoTI1 under salt, drought and abscisic acid treatment suggested that CoTI1 might play important role in the resistance against abiotic stress.