Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/88151
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dc.contributor.authorKumari, Geetaen
dc.contributor.authorWong, Ka Hoen
dc.contributor.authorSerra, Aidaen
dc.contributor.authorShin, Joonen
dc.contributor.authorYoon, Ho Supen
dc.contributor.authorSze, Siu Kwanen
dc.contributor.authorTam, James P.en
dc.date.accessioned2018-08-20T04:36:26Zen
dc.date.accessioned2019-12-06T16:57:11Z-
dc.date.available2018-08-20T04:36:26Zen
dc.date.available2019-12-06T16:57:11Z-
dc.date.issued2018en
dc.identifier.citationKumari, 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-yen
dc.identifier.urihttps://hdl.handle.net/10356/88151-
dc.identifier.urihttp://hdl.handle.net/10220/45615en
dc.description.abstractBackground: 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.en
dc.description.sponsorshipMOE (Min. of Education, S’pore)en
dc.format.extent13 p.en
dc.language.isoenen
dc.relation.ispartofseriesBMC Plant Biologyen
dc.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.en
dc.subjectDRNTU::Science::Biological sciences::Botanyen
dc.subjectJasmintidesen
dc.subjectCysteine-rich Peptidesen
dc.titleMolecular diversity and function of jasmintides from Jasminum sambacen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1186/s12870-018-1361-yen
dc.description.versionPublished versionen
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