Evidence map›Paper›PMID 39777642›Full record

ArticleApplied biochemistry and biotechnology2025

Succinylome Profiling the Function and Distribution of Lysine Succinylation in Saccharopolyspora erythraea.

Xiang Ke, Xing Jiang, Muhammad Hammad Hussain, Xiwei Tian, Ju Chu

Abstract read
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In one paragraph

Article in Applied biochemistry and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

5 authors.

Xiang KeState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
Xing JiangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
Muhammad Hammad HussainState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
Xiwei TianState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China. xiweitian@ecust.edu.cn.
Ju ChuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China. juchu@ecust.edu.cn.ORCID http://orcid.org/0000-0002-6406-1748

Funding

Key Technologies Research and Development Program 2022YFC2105403National Natural Science Foundation of China 21276081
6 · The paper itself

Abstract

As a novel protein post-translational modification, lysine succinylation is widely involved in metabolism regulation. To describe succinylated lysine's physiological functions and distribution patterns in Saccharopolyspora erythraea, a large and global protein succinylome was identified in a hypersuccinylated strain E3ΔsucC, using high-resolution 4D label-free mass spectrometry. Bioinformatic analysis was conducted to examine the succinylated proteins further in this study. The results showed that succinylated proteins were identified to be predominantly involved in protein synthesis, central carbon and nitrogen metabolism, and secondary metabolism. The process of lysine succinylation was found intricately regulated by a delicate interplay of factors, such as the relative abundance of lysine within the protein, the strategic positioning of polar amino acids flanking the succinylated sites, and the degree to which lysine residues are exposed to the solvent, thereby shaping the landscape of post-translational modifications. This systematic analysis has represented the global analysis of lysine succinylation in S. erythraea and has provided an important resource for exploring the function and regulation of lysine succinylation in S. erythraea and likely in all actinomycetes.

Indexed as

Bacterial ProteinsLysineProtein Processing, Post-TranslationalSaccharopolysporaSuccinic AcidBacterial ProteinsLysineSuccinic AcidLysine succinylationPost-translational modificationSaccharopolyspora erythraeaSuccinylome

Identifiers

PMID39777642

What OpenQuestion holds

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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.