Figure S3. NOE cross peak between the HÎ˛s of the each disulfide bond in jS3. (DOCX 171 kb

Aida Serra (1476244)

Geeta Kumari (1476247)

Ho Yoon (3745087)

James Tam (639411)

Joon Shin (643333)

Ka Wong (3582938)

Siu Sze (3476045)

BMC Plant Biology

Figure S2. Summary of sequential and medium NOE connectivity. Slowly exchanging amide protons (filled box) and backbone vicinal coupling constants (open circle: 3JHNα < 6 Hz, filled circle: 3JHNα > 8 Hz) are indicated. (DOCX 4739 kb

FigShare

Additional file 3: of Molecular diversity and function of jasmintides from Jasminum sambac

Figure S1. NH/CÎąH fingerprint region of 2D-NOESY spectrum of jS3 recorded in 90% H2O/10% D2O at 298Â K. Sequential connectivity of each amino acid residue are shown by solid lines. (DOCX 4392 kb

Additional file 2: of Molecular diversity and function of jasmintides from Jasminum sambac

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.MOE (Min. of Education, S’pore)Published versio

Kumari, Geeta

Wong, Ka Ho

Serra, Aida

Shin, Joon

Yoon, Ho Sup

Sze, Siu Kwan

Tam, James P.

Digital Repository - Nanyang Technological University

Molecular diversity and function of jasmintides from Jasminum sambac

Figure S6. The effect of jasmintide jS3 on the cell viability of Sf9 cells. (DOCX 111 kb

Additional file 8: of Molecular diversity and function of jasmintides from Jasminum sambac

DR-NTU (Digital Repository of NTU)

Additional file 4: of Molecular diversity and function of jasmintides from Jasminum sambac

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

Geeta Kumari

Ka Ho Wong

Aida Serra

Joon Shin

Ho Sup Yoon

Siu Kwan Sze

James P. Tam

Directory of Open Access Journals

https://figshare.com/articles/Additional_file_2_of_Molecular_diversity_and_function_of_jasmintides_from_Jasminum_sambac/6808190

Additional file 4: of Molecular diversity and function of jasmintides from Jasminum sambac

Abstract

Similar works

Full text

Available Versions

FigShare

FigShare

Digital Repository - Nanyang Technological University

FigShare

DR-NTU (Digital Repository of NTU)

FigShare

Directory of Open Access Journals