Evidence map›Paper›PMID 39011828›Full record

ArticleMolecular plant pathology2024

A cyclic di-GMP-binding adaptor protein interacts with a N5-glutamine methyltransferase to regulate the pathogenesis in Xanthomonas citri subsp. citri.

Yu Shi, Tianfang Cheng, Qing Wei Cheang, Xiaoyan Zhao, Zeling Xu, Zhao-Xun Liang, Linghui Xu, Junxia Wang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular plant pathology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Pathogens (Basel, Switzerland) · 2026
    Review
  2. Article
  3. Article
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.

Yu ShiIntegrative Microbiology Research Centre, Guangdong Province Key Laboratory of Microbial Signals and Disease Control, South China Agricultural University, Guangzhou, China.
Tianfang ChengIntegrative Microbiology Research Centre, Guangdong Province Key Laboratory of Microbial Signals and Disease Control, South China Agricultural University, Guangzhou, China.
Qing Wei CheangSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Xiaoyan ZhaoIntegrative Microbiology Research Centre, Guangdong Province Key Laboratory of Microbial Signals and Disease Control, South China Agricultural University, Guangzhou, China.
Zeling XuIntegrative Microbiology Research Centre, Guangdong Province Key Laboratory of Microbial Signals and Disease Control, South China Agricultural University, Guangzhou, China.
Zhao-Xun LiangSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Linghui XuIntegrative Microbiology Research Centre, Guangdong Province Key Laboratory of Microbial Signals and Disease Control, South China Agricultural University, Guangzhou, China.
Junxia WangIntegrative Microbiology Research Centre, Guangdong Province Key Laboratory of Microbial Signals and Disease Control, South China Agricultural University, Guangzhou, China.ORCID 0000-0001-5020-8959

Funding

The Basic and Applied basic Research Project of Guangzhou basic Research Program, China 202201010058The Natural Science Foundation of Guangdong Province, China 2021A1515010761The Natural Science Foundation of Guangdong Province, China 2022A1515010869
6 · The paper itself

Abstract

The second messenger cyclic diguanylate monophosphate (c-di-GMP) regulates a wide range of bacterial behaviours through diverse mechanisms and binding receptors. Single-domain PilZ proteins, the most widespread and abundant known c-di-GMP receptors in bacteria, act as trans-acting adaptor proteins that enable c-di-GMP to control signalling pathways with high specificity. This study identifies a single-domain PilZ protein, XAC3402 (renamed N5MapZ), from the phytopathogen Xanthomonas citri subsp. citri (Xcc), which modulates Xcc virulence by directly interacting with the methyltransferase HemK. Through yeast two-hybrid, co-immunoprecipitation and immunofluorescent staining, we demonstrated that N5MapZ and HemK interact directly under both in vitro and in vivo conditions, with the strength of the protein-protein interaction decreasing at high c-di-GMP concentrations. This finding distinguishes N5MapZ from other characterized single-domain PilZ proteins, as it was previously known that c-di-GMP enhances the interaction between those single-domain PilZs and their protein partners. This observation is further supported by the fact that the c-di-GMP binding-defective mutant N5MapZ

Indexed as

Bacterial ProteinsCyclic GMPMethyltransferasesXanthomonasPlant DiseasesProtein BindingVirulenceBacterial Proteinsbis(3',5')-cyclic diguanylic acidCyclic GMPMethyltransferasescyclic di‐GMPexoenzymeHemKmotilityPrfAstress tolerancevirulenceXanthomonas citri subsp. citri

Identifiers

PMID39011828
PMCPMC11250160

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Registered trials

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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.