First Succinyl-Proteome Profiling of Extensively Drug-Resistant Mycobacterium tuberculosis Revealed Involvement of Succinylation in Cellular Physiology
Abstract
Protein lysine succinylation, an emerging protein post-translational modification widespread among eukaryotic and prokaryotic cells, represents an important regulator of cellular processes. However, the extent and function of lysine succinylation in Mycobacterium tuberculosis, especially extensively drug-resistant strain, remain elusive. Combining protein/peptide prefractionation, immunoaffinity enrichment, and LC-MS/MS analysis, a total of 686 succinylated proteins and 1739 succinylation sites of M. tuberculosis were identified, representing the first global profiling of M. tuberculosis lysine succinylation. The identified succinylated proteins are involved in a variety of cellular functions such as metabolic processes, transcription, translation, and stress responses and exhibit different subcellular localization via GO, protein interaction network, and other bioinformatic analysis. Notably, proteins involved in protein biosynthesis and carbon metabolism are preferred targets of lysine succinylation. Moreover, two prevalent sequence patterns: EK(suc) and K*****K(suc), can be found around the succinylation sites. There are 109 lysine-succinylated homologues in E. coli, suggesting highly conserved succinylated proteins. Succinylation was found to occur at the active sites predicted by Prosite signature including Rv0946c, indicating that lysine succinylation may affect their activities. There is extensive overlapping between acetylation sites and succinylation sites in M. tuberculosis. Many M. tuberculosis metabolic enzymes and antibiotic resistance proteins were succinylated. This study provides a basis for further characterization of the pathophysiological role of lysine succinylation in M. tuberculosis.
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- Authors
- Xie, L., Liu, W., Li, Q., Chen, S., Xu, M., Huang, Q., Zeng, J., Zhou, M., & Xie, J.
- Affiliations
- Southwest University (CN)
- Fudan University (CN)
- Zhejiang Entry-Exit Inspection and Quarantine Bureau (CN)
- Corresponding author
- Xie, Jianping
- ORCID
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-11-12
- Volume
- 14
- Issue
- 1
- Pages
- 107-119
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2028938598
- Cited by
- 128
- References
- 35
- Citations by year
- 2026: 2 · 2025: 8 · 2024: 10 · 2023: 3 · 2022: 16 · 2021: 18 · 2020: 9 · 2019: 17 · 2018: 12 · 2017: 12 · 2016: 16 · 2015: 5
- FWCI
- 7.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Proteome Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education of the People's Republic of China (NCET-11-0703, XDJK2011D006, XDJK2012D007, XDJK2012D011, XDJK2013D003, XDJK2014D040)
- National Natural Science Foundation of China (81071316, 81271882, 81301394, 81371851)
- Undergraduates Teaching Reform Program (2013JY201)
- National Megaprojects for Key Infectious Diseases (2008ZX10003-006)
- Chongqing Municipal Committee of Education (YJG123104)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Mycobacterium tuberculosis, lysine succinylation, succinylation, extensively drug-resistant tuberculosis, post-translational modification, succinylome, protein synthesis, carbon metabolism, stress response, acetylation, metabolic enzymes, subcellular localization
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Molecular Sequence Data, Mycobacterium tuberculosis, Protein Processing, Post-Translational, Succinates, Protein Structure, Secondary, Proteome, Drug Resistance, Multiple, Bacterial, Metabolic Networks and Pathways, Protein Interaction Maps
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