Evidence map›Paper›PMID 25605462›Full record

ArticleMolecular & cellular proteomics : MCP2015

Succinylome analysis reveals the involvement of lysine succinylation in metabolism in pathogenic Mycobacterium tuberculosis.

Mingkun Yang, Yan Wang, Ying Chen, Zhongyi Cheng, Jing Gu, Jiaoyu Deng, Lijun Bi, Chuangbin Chen, Ran Mo, Xude Wang and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
6.8field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 133 citations in OpenAlex.

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  14. Acetylome and Succinylome Profiling ofAntibiotics (Basel, Switzerland) · 2022
    Article
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5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 1 country.

Mingkun YangFrom the ‡Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China;
Yan WangFrom the ‡Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China;
Ying ChenFrom the ‡Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China;
Zhongyi Cheng§Advanced Institute of Translational Medicine, Tongji University, Shanghai 200092, China;
Jing Gu¶Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China;
Jiaoyu Deng¶Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China;
Lijun Bi‖Key Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China;
Chuangbin Chen**Jingjie PTM Biolabs (Hangzhou) Co. Ltd, Hangzhou 310018, China.
Ran MoFrom the ‡Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China;
Xude Wang¶Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China;
Feng GeFrom the ‡Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China; gefeng@ihb.ac.cn.
Institute of Hydrobiology · CNChinese Academy of Sciences · CNWuhan Institute of Virology · CNTongji University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycobacterium tuberculosis (Mtb), the causative agent of human tuberculosis, remains one of the most prevalent human pathogens and a major cause of mortality worldwide. Metabolic network is a central mediator and defining feature of the pathogenicity of Mtb. Increasing evidence suggests that lysine succinylation dynamically regulates enzymes in carbon metabolism in both bacteria and human cells; however, its extent and function in Mtb remain unexplored. Here, we performed a global succinylome analysis of the virulent Mtb strain H37Rv by using high accuracy nano-LC-MS/MS in combination with the enrichment of succinylated peptides from digested cell lysates and subsequent peptide identification. In total, 1545 lysine succinylation sites on 626 proteins were identified in this pathogen. The identified succinylated proteins are involved in various biological processes and a large proportion of the succinylation sites are present on proteins in the central metabolism pathway. Site-specific mutations showed that succinylation is a negative regulatory modification on the enzymatic activity of acetyl-CoA synthetase. Molecular dynamics simulations demonstrated that succinylation affects the conformational stability of acetyl-CoA synthetase, which is critical for its enzymatic activity. Further functional studies showed that CobB, a sirtuin-like deacetylase in Mtb, functions as a desuccinylase of acetyl-CoA synthetase in in vitro assays. Together, our findings reveal widespread roles for lysine succinylation in regulating metabolism and diverse processes in Mtb. Our data provide a rich resource for functional analyses of lysine succinylation and facilitate the dissection of metabolic networks in this life-threatening pathogen.

Indexed as

MetabolomeAcetate-CoA LigaseAmino Acid MotifsAmino Acid SequenceBacterial ProteinsBlotting, WesternCarbonConserved SequenceHumansImmunoblottingImmunoprecipitationLysineMetabolomicsMolecular Dynamics SimulationMolecular Sequence AnnotationMolecular Sequence DataAcetate-CoA LigaseBacterial ProteinsCarbonLysineNADSuccinates

Identifiers

PMID25605462
PMCPMC4390261
OpenAlexW2108752167

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.