Please use this identifier to cite or link to this item:
https://hdl.handle.net/10356/88151
Title: | Molecular diversity and function of jasmintides from Jasminum sambac | Authors: | Kumari, Geeta Wong, Ka Ho Serra, Aida Shin, Joon Yoon, Ho Sup Sze, Siu Kwan Tam, James P. |
Keywords: | DRNTU::Science::Biological sciences::Botany Jasmintides Cysteine-rich Peptides |
Issue Date: | 2018 | Source: | Kumari, G., Wong, K. H., Serra, A., Shin, J., Yoon, H. S., Sze, S. K., & Tam, J. P. (2018). Molecular diversity and function of jasmintides from Jasminum sambac. BMC Plant Biology, 18(1), 144. doi:10.1186/s12870-018-1361-y | Series/Report no.: | BMC Plant Biology | Abstract: | Background: Jasmintides jS1 and jS2 from Jasminum sambac were previously identified as a novel family of cysteine-rich peptides (CRPs) with an unusual disulfide connectivity. However, very little else is known about jasmintides, particularly their molecular diversity and functions. Here, we report the discovery and characterization of a novel suite of jasmintides from J. sambac using transcriptomic, peptidomic, structural and functional tools. Results: Transcriptomic analysis of leaves, flowers and roots revealed 14 unique jasmintide precursors, all of which possess a three-domain architecture comprising a signal peptide, a pro-domain and a mature jasmintide domain. Peptidomic analysis, using fractionated mixtures of jasmintides and chemical derivatization of cysteine to pseudolysine, trypsin digestion and MS/MS sequencing, revealed an additional 86 jasmintides, some of which were post-translationally modified. NMR analysis showed that jasmintide jS3 has three anti-parallel β-strands with a three-disulfide connectivity of CysI−CysV, CysII−CysIV and CysIII−CysVI, which is similar to jasmintide jS1. Jasmintide jS3 was able to withstand thermal, acidic and enzymatic degradation and, importantly, exhibited antifeedant activity against mealworm Tenebrio molitor. Conclusion: Together, this study expands the existing library of jasmintides and furthers our understanding of the molecular diversity and cystine framework of CRPs as scaffolds and tools for engineering peptides targeting pests. | URI: | https://hdl.handle.net/10356/88151 http://hdl.handle.net/10220/45615 |
DOI: | 10.1186/s12870-018-1361-y | Schools: | School of Biological Sciences | Rights: | © 2018 The Author(s). This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. | Fulltext Permission: | open | Fulltext Availability: | With Fulltext |
Appears in Collections: | SBS Journal Articles |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Molecular diversity and function of jasmintides from Jasminum sambac.pdf | 4.21 MB | Adobe PDF | View/Open |
SCOPUSTM
Citations
50
9
Updated on Mar 12, 2024
Web of ScienceTM
Citations
50
5
Updated on Oct 30, 2023
Page view(s) 50
476
Updated on Mar 19, 2024
Download(s) 50
130
Updated on Mar 19, 2024
Google ScholarTM
Check
Altmetric
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.