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Unrestrictive identification of post-translational modifications in Hevea brasiliensis latex.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Habib, Mohd Afiq Hazlami Gan, Chee-Yuen Latiff, Aishah Abdul Ismail, Mohd Nazri |
| Copyright Year | 2018 |
| Abstract | The natural rubber latex extracted from the bark of Hevea brasiliensis plays various important roles in modern society. Post-translational modifications (PTMs) of the latex proteins are important for the stability and functionality of the proteins. In this study, latex proteins were acquired from the C-serum, lutoids, and rubber particle layers of latex without using prior enrichment steps; they were fragmented using collision-induced dissociation (CID), higher-energy collisional dissociation (HCD), and electron-transfer dissociation (ETD) activation methods. PEAKS 7 were used to search for unspecified PTMs, followed by analysis through PTM prediction tools to crosscheck both results. There were 73 peptides in 47 proteins from H. brasiliensis protein sequences derived from UniProtKB were identified and predicted to be post-translationally modified. The peptides with PTMs identified include phosphorylation, lysine acetylation, N-terminal acetylation, hydroxylation, and ubiquitination. Most of the PTMs discovered have yet to be reported in UniProt, which would provide great assistance in the research of the functional properties of H. brasiliensis latex proteins, as well as being useful biomarkers. The data are available via the MassIVE repository with identifier MSV000082419. |
| Starting Page | 1 |
| Ending Page | 7 |
| Page Count | 7 |
| File Format | PDF HTM / HTML |
| DOI | 10.1139/bcb-2018-0020 |
| PubMed reference number | 30058361 |
| Journal | Medline |
| Alternate Webpage(s) | https://tspace.library.utoronto.ca/bitstream/1807/92500/1/bcb-2018-0020.pdf |
| Journal | Biochemistry and cell biology = Biochimie et biologie cellulaire |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |