Evidence map›Paper›PMID 38066175›Full record

ArticleCommunications biology2023

Post-crotonylation oxidation by a monooxygenase promotes acetyl-CoA synthetase degradation in Streptomyces roseosporus.

Bing-Bing Ma, Chen-Fan Sun, Jing-Yi Zhou, Shuai-Lei Gu, Xin-Yi Dai, Yan-Zhen Chen, Qing-Wei Zhao, Xu-Ming Mao

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

8 authors at 3 institutions in 1 country.

Bing-Bing Ma *Department of Clinical Pharmacy, the First Affiliated Hospital & Institute of Pharmaceutical Biotechnology, School of Medicine, Zhejiang University, 310058, Hangzhou, China.
Chen-Fan Sun *Department of Clinical Pharmacy, the First Affiliated Hospital & Institute of Pharmaceutical Biotechnology, School of Medicine, Zhejiang University, 310058, Hangzhou, China.
Jing-Yi Zhou *Department of Clinical Pharmacy, the First Affiliated Hospital & Institute of Pharmaceutical Biotechnology, School of Medicine, Zhejiang University, 310058, Hangzhou, China.
Shuai-Lei GuCollege of Life Sciences, Zhejiang University, 310058, Hangzhou, China.
Xin-Yi DaiCollege of Life Sciences, Zhejiang University, 310058, Hangzhou, China.
Yan-Zhen ChenCollege of Life Sciences, Zhejiang University, 310058, Hangzhou, China.
Qing-Wei ZhaoDepartment of Clinical Pharmacy, the First Affiliated Hospital & Institute of Pharmaceutical Biotechnology, School of Medicine, Zhejiang University, 310058, Hangzhou, China. qwzhao@zju.edu.cn.
Xu-Ming MaoDepartment of Clinical Pharmacy, the First Affiliated Hospital & Institute of Pharmaceutical Biotechnology, School of Medicine, Zhejiang University, 310058, Hangzhou, China. xmmao@zju.edu.cn.ORCID 0000-0003-0669-7630
Zhejiang University · CNNational Medical Products Administration · CNZhejiang Provincial Institute of Communications Planning,Design & Research · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32070039
6 · The paper itself

Abstract

Protein post-translational modifications (PTMs) with various acyl groups play central roles in Streptomyces. But whether these acyl groups can be further modified, and the influences of these potential modifications on bacterial physiology have not been addressed. Here in Streptomyces roseosporus with rich crotonylation, a luciferase monooxygenase LimB is identified to elaborately regulate the crotonylation level, morphological development and antibiotic production by oxidation on the crotonyl groups of an acetyl-CoA synthetase Acs. This chemical modification on crotonylation leads to Acs degradation via the protease ClpP1/2 pathway and lowered intracellular crotonyl-CoA pool. Thus, we show that acyl groups after PTMs can be further modified, herein named post-PTM modification (PPM), and LimB is a PTM modifier to control the substrate protein turnover for cell development of Streptomyces. These findings expand our understanding of the complexity of chemical modifications on proteins for physiological regulation, and also suggest that PPM would be widespread.

Indexed as

LigasesStreptomycesAcetyl Coenzyme AMixed Function OxygenasesProteinsAcetyl Coenzyme ALigasesMixed Function OxygenasesProteins

Identifiers

PMID38066175
PMCPMC10709465
OpenAlexW4389490633

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.