Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii
Lysine malonylation (Kmal) is a new post-translational modification (PTM), which has been reported in several prokaryotic and eukaryotic species. Although Kmal can regulate many and diverse biological processes in various organisms, knowledge about this important PTM in the apicomplexan parasite Tox...
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Frontiers Media S.A.
2020-04-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fmicb.2020.00776/full |
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| author | Lan-Bi Nie Lan-Bi Nie Qin-Li Liang Rui Du Hany M. Elsheikha Nai-Jian Han Fa-Cai Li Xing-Quan Zhu |
| author_facet | Lan-Bi Nie Lan-Bi Nie Qin-Li Liang Rui Du Hany M. Elsheikha Nai-Jian Han Fa-Cai Li Xing-Quan Zhu |
| author_sort | Lan-Bi Nie |
| collection | DOAJ |
| description | Lysine malonylation (Kmal) is a new post-translational modification (PTM), which has been reported in several prokaryotic and eukaryotic species. Although Kmal can regulate many and diverse biological processes in various organisms, knowledge about this important PTM in the apicomplexan parasite Toxoplasma gondii is limited. In this study, we performed the first global profiling of malonylated proteins in T. gondii tachyzoites using affinity enrichment and Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. Three experiments performed in tandem revealed 294, 345, 352 Kmal sites on 203, 236, 230 malonylated proteins, respectively. Computational analysis showed the identified malonylated proteins to be localized in various subcellular compartments and involved in many cellular functions, particularly mitochondrial function. Additionally, one conserved Kmal motif with a strong bias for cysteine was detected. Taken together, these findings provide the first report of Kmal profile in T. gondii and should be an important resource for studying the physiological roles of Kmal in this parasite. |
| first_indexed | 2024-12-19T06:27:40Z |
| format | Article |
| id | doaj.art-0af9b6b3d5f44f4f95bf9eac3197d1e4 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-19T06:27:40Z |
| publishDate | 2020-04-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-0af9b6b3d5f44f4f95bf9eac3197d1e42022-12-21T20:32:29ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2020-04-011110.3389/fmicb.2020.00776525200Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondiiLan-Bi Nie0Lan-Bi Nie1Qin-Li Liang2Rui Du3Hany M. Elsheikha4Nai-Jian Han5Fa-Cai Li6Xing-Quan Zhu7College of Animal Science and Technology, Jilin Agricultural University, Changchun, ChinaState Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, ChinaState Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, ChinaCollege of Animal Science and Technology, Jilin Agricultural University, Changchun, ChinaFaculty of Medicine and Health Sciences, School of Veterinary Medicine and Science, University of Nottingham, Sutton Bonington Campus, Loughborough, United KingdomJingjie PTM Biolabs (Hangzhou) Co. Ltd., Hangzhou, ChinaState Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, ChinaState Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, ChinaLysine malonylation (Kmal) is a new post-translational modification (PTM), which has been reported in several prokaryotic and eukaryotic species. Although Kmal can regulate many and diverse biological processes in various organisms, knowledge about this important PTM in the apicomplexan parasite Toxoplasma gondii is limited. In this study, we performed the first global profiling of malonylated proteins in T. gondii tachyzoites using affinity enrichment and Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. Three experiments performed in tandem revealed 294, 345, 352 Kmal sites on 203, 236, 230 malonylated proteins, respectively. Computational analysis showed the identified malonylated proteins to be localized in various subcellular compartments and involved in many cellular functions, particularly mitochondrial function. Additionally, one conserved Kmal motif with a strong bias for cysteine was detected. Taken together, these findings provide the first report of Kmal profile in T. gondii and should be an important resource for studying the physiological roles of Kmal in this parasite.https://www.frontiersin.org/article/10.3389/fmicb.2020.00776/fullToxoplasma gondiitoxoplasmosispost-translational modificationslysine malonylationmalonylome |
| spellingShingle | Lan-Bi Nie Lan-Bi Nie Qin-Li Liang Rui Du Hany M. Elsheikha Nai-Jian Han Fa-Cai Li Xing-Quan Zhu Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii Frontiers in Microbiology Toxoplasma gondii toxoplasmosis post-translational modifications lysine malonylation malonylome |
| title | Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii |
| title_full | Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii |
| title_fullStr | Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii |
| title_full_unstemmed | Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii |
| title_short | Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii |
| title_sort | global proteomic analysis of lysine malonylation in toxoplasma gondii |
| topic | Toxoplasma gondii toxoplasmosis post-translational modifications lysine malonylation malonylome |
| url | https://www.frontiersin.org/article/10.3389/fmicb.2020.00776/full |
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