Evidence map›Paper›PMID 38750524›Full record

ArticleBMC biology2024

The crotonylated and succinylated proteins of jujube involved in phytoplasma-stress responses.

Liman Zhang, Huibin Wang, Chaoling Xue, Yin Liu, Yao Zhang, Zhiguo Liu, Xiangrui Meng, Mengjun Liu, Jin Zhao

Abstract read
In one paragraph

Article in BMC biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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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

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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

2 citing papers in PubMed.

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4 · The record

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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

9 authors.

Liman ZhangCollege of Life Science, Hebei Agricultural University, Baoding, China.
Huibin WangCollege of Life Science, Hebei Agricultural University, Baoding, China.
Chaoling XueCollege of Life Science, Hebei Agricultural University, Baoding, China.
Yin LiuCollege of Life Science, Hebei Agricultural University, Baoding, China.
Yao ZhangCollege of Life Science, Hebei Agricultural University, Baoding, China.
Zhiguo LiuResearch Center of Chinese Jujube, Hebei Agricultural University, Baoding, China.
Xiangrui MengCollege of Life Science, Hebei Agricultural University, Baoding, China.
Mengjun LiuResearch Center of Chinese Jujube, Hebei Agricultural University, Baoding, China. kjliu@hebau.edu.cn.
Jin ZhaoCollege of Life Science, Hebei Agricultural University, Baoding, China. zhaojinbd@126.com.ORCID http://orcid.org/0000-0002-6035-1828

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProtein posttranslational modifications (PTMs) are fast and early responses to environmental changes, including pathogen infection. Jujube witches' broom (JWB) is a phytoplasma disease causing great economic loss in jujube production. After phytoplasma infection, the transcriptional, translational, and metabolic levels in jujube were activated, enabling it to survive during phytoplasma invasion. However, no study has yet reported on PTMs in jujube. Lysine crotonylation (Kcr) and lysine succinylation (Ksu) have been popular studies in recent years and their function in plant phytoplasma-stress responses remains unclear.

resultsHere, 1656 crotonylated and 282 succinylated jujube proteins were first identified under phytoplasma-stress, of which 198 were simultaneously crotonylated and succinylated. Comparative analysis revealed that 656 proteins, 137 crotonylated and 43 succinylated proteins in jujube were regulated by phytoplasma infection, suggesting that Kcr was more universal than Ksu. Kcr differentially expressed proteins (DEPs) were related to ribosomes, photosynthetic and carbon metabolism, while Ksu DEPs were mainly involved in carbon metabolism, the TCA cycle and secondary metabolite biosynthesis. The crosstalk network among proteome, crotonylome and succinylome showed that DEPs related to ribosomal, peroxidases and glutathione redox were enriched. Among them, ZjPOD51 and ZjPHGPX2 significantly increased at the protein and Kcr level under phytoplasma-stress. Notably, 7 Kcr sites were identified in ZjPHGPX2, a unique antioxidant enzyme. After inhibitor nicotinamide (NAM) treatment, GPX enzyme activity in jujube seedlings was reduced. Further, site-directed mutagenesis of key Kcr modification sites K130 and/or K135 in ZjPHGPX2 significantly reduced its activity.

conclusionsThis study firstly provided large-scale datasets of Kcr and Ksu in phytoplasma-infected jujube and revealed that Kcr modification in ZjPHGPX2 positively regulates its activity.

Indexed as

PhytoplasmaPlant DiseasesPlant ProteinsZiziphusLysineProtein Processing, Post-TranslationalStress, PhysiologicalLysinePlant ProteinsCrotonylomeEnzyme activityInhibitor NAMJujube phloemPhytoplasma-stressSite-directed mutagenesisSuccinylomeZjPHGPX2

Identifiers

PMID38750524
PMCPMC11094900

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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.