Evidence map›Paper›PMID 40327119›Full record

ArticleCurrent microbiology2025

A Methyl-Accepting Chemotaxis Protein MCP-5685 Associated with Indole Synthesis in Pantoea ananatis YJ76 Influences its Plant Growth-Promoting Potential and Adaptability to Stress Conditions.

Haotian Zhang, Xinyi Zhou, Xueying Wang, Jing Zheng, Yongjun Feng

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Article in Current microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

5 authors.

Haotian ZhangSchool of Life Science, Beijing Institute of Technology, Beijing, China.
Xinyi ZhouSchool of Life Science, Beijing Institute of Technology, Beijing, China.
Xueying WangSchool of Life Science, Beijing Institute of Technology, Beijing, China.
Jing ZhengSchool of Life Science, Beijing Institute of Technology, Beijing, China.
Yongjun FengSchool of Life Science, Beijing Institute of Technology, Beijing, China. fengyj@bit.edu.cn.ORCID http://orcid.org/0000-0002-7830-3023

Funding

National Key Research and Development Program of China 2018YFA0901800National Natural Science Foundation of China 31870090
6 · The paper itself

Abstract

Pantoea ananatis YJ76 is a predominant endophytic diazotrophic bacterium isolated from rice, which can produce indole as a signal to improve stress resistance, colonization, and growth-promoting effect on the host. Methyl-accepting chemotaxis proteins (MCPs) are the main chemoreceptor in bacteria and participate in regulating various cellular activities. By constructing an mTn5 transposon mutant library of YJ76, we screened out a mutant with decreased indole production. And its ability to resist stresses and starvation, as well as colonizing and growth-promoting effect on host rice plants, was inhibited. Using the hiTAIL-PCR technique combined the genome re-sequencing, the mutation site was identified as the mcp-5685 gene with a length of 1545 bp. Bioinformatics analysis and chemotaxis experiments showed that the MCP encoded by mcp-5685 had L-serine chemotaxis functions, revealing the mechanism of the gene encoding protein to drive L-serine uptake, a key component for tryptophan synthesis, and thus promote indole synthesis in the regulatory pathways for indole synthesis. Starting from the upstream regulation direction of indole synthesis, this study breaks through the previous researching limitation of focusing only on the downstream physiological function regulation of indole and provides new ideas for studying the indole signal.

Indexed as

Bacterial ProteinsIndolesMethyl-Accepting Chemotaxis ProteinsOryzaPantoeaAdaptation, PhysiologicalChemotaxisGene Expression Regulation, BacterialStress, PhysiologicalBacterial ProteinsindoleIndolesMethyl-Accepting Chemotaxis Proteins

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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.