Quantitative comparison of phospho-proteins of <i>Mycolicibacterium smegmatis</i> at different growing phases.

Danyang XU; Yuan GAO; Jiahui SHI; Songhao JIANG; Yu XUE; Yao ZHANG

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Quantitative comparison of phospho-proteins of Mycolicibacterium smegmatis at different growing phases.

Author: Danyang XU ¹ ; Yuan GAO ² ; Jiahui SHI ³ ; Songhao JIANG ³ ; Yu XUE ¹ ; Yao ZHANG ³
Author Information

1. School of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, Hubei, China.
2. Central Laboratory of College of Horticulture, Nanjing Agricultural University, Nanjing 210095, Jiangsu, China.
3. State Key Laboratory of Medical Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Research Unit of Proteomics & Research and Development of New Drug of Chinese Academy of Medical Sciences, Academy of Military Medical Sciences of Academy of Military Science, Beijing 102206, China.
Publication Type:Comparative Study
Keywords: Mycolicibacterium smegmatis; cell division; cell elongation; quantitative phosphoproteomics
MeSH: Mycobacterium smegmatis/genetics*; Bacterial Proteins/genetics*; Phosphorylation; Phosphoproteins/metabolism*; Mycobacterium tuberculosis/growth & development*; Proteome/metabolism*; Proteomics
From: Chinese Journal of Biotechnology 2024;40(11):4098-4110
CountryChina
Language:Chinese
Abstract: Protein phosphorylation plays a key role in Mycobacterium tuberculosis, the pathogen of tuberculosis, holding promise as a new target of anti-tuberculosis drugs. We used M. smegmatis, a close relative of M. tuberculosis, as a model organism to study the protein phosphorylation at different growth phases. We identified 573 phosphorylated peptides and 816 phosphorylated sites of 385 proteins in the M. smegmatis samples at both logarithmic and stationary phases, and then established a comprehensive dataset of phosphorylated proteins in M. smegmatis. By comparing the expression levels of phosphorylated proteins between the logarithmic and the stationary phase with the selected ion monitoring (SIM) strategy, we verified 68 upregulated proteins involved in cell division and protein translation, and 69 downregulated proteins mainly involved in the tricarboxylic acid cycle pathway. The differentially expressed phosphorylated proteins were significantly enriched in important cellular cycle events such as cell elongation and division. The findings of this study provide proteome evidence for elucidating the phosphorylation in both M. smegmatis and M. tuberculosis.