Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2025 Mar 16;47(3):195.
doi: 10.3390/cimb47030195.

Genome-Wide Identification of β-Ketoacyl CoA Synthase Gene Family in Melon (Cucumis melo L.) and Its Expression Analysis in Autotoxicity, Saline-Alkali, and Microplastic Exposure Environments

Affiliations

Genome-Wide Identification of β-Ketoacyl CoA Synthase Gene Family in Melon (Cucumis melo L.) and Its Expression Analysis in Autotoxicity, Saline-Alkali, and Microplastic Exposure Environments

Lizhen Zhang et al. Curr Issues Mol Biol. .

Abstract

β-ketoacyl CoA synthase (KCS) is a key enzyme in the synthesis of long-chain fatty acids. It affects plant stress resistance by regulating the chain length of fatty acid elongation products, the wax deposition in plant epidermis, and the formation of suberization layers. Through a comprehensive, genome-wide analysis, we identified members of the melon KCS (CmKCS) family and characterized their sequence features, phylogenetic relationships, and expression profiles under three abiotic stress conditions, employing bioinformatics tools and methods. Fifteen CmKCSs were identified in the melon genome and found to be unevenly distributed across eight chromosomes. The subcellular localization of most members is located on the cytoplasmic membrane and chloroplasts. The CmKCS family amplifies its members in a tandem repeat manner, which is more closely related to the cucumber KCS and has similar gene functions. Subfamilies I, IV, and VI exhibit variations in conserved domain sequences, which may indicate specific functional differentiation. The promoter region harbors various cis-acting elements related to plant hormones and abiotic stress responses. Among these, the most abundant are elements responsive to abscisic acid, methyl jasmonate, salicylic acid, and anaerobic induction. CmKCS5, CmKCS6, CmKCS10, and CmKCS12 showed high expression in autotoxicity, saline-alkali stress, and microplastic exposure environments. These four CmKCSs may play important roles in melon development and stress response. In conclusion, this study provides a comprehensive analysis of the CmKCS gene family, revealing its potential roles in melon's response to abiotic stresses and laying a foundation for further functional characterization of these genes in stress tolerance mechanisms.

Keywords: cucurbits; molecular phylogeny; stress response gene; very-long-chain fatty acids; β-ketoacyl CoA synthase gene.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
Chromosomal localization of KCSs in melon.
Figure 2
Figure 2
Phylogenetic tree of KCSs in melon and other plants.
Figure 3
Figure 3
Phylogenetic relationships (A), motif composition (B), and gene structure (C) of KCSs in melon.
Figure 4
Figure 4
Collinearity analysis of KCSs in melon.
Figure 5
Figure 5
Collinearity analysis of KCSs of 7 species.
Figure 6
Figure 6
Phylogenetic relationships (A), the site (B), and number (C) of Cis-acting elements in melon KCSs promoter.
Figure 7
Figure 7
Differential expression of KCSs in melon under three abiotic stresses.

References

    1. Haslam T.M., Kunst L. Extending the story of very-long-chain fatty acid elongation. Plant Sci. 2013;210:93–107. doi: 10.1016/j.plantsci.2013.05.008. - DOI - PubMed
    1. Lewandowska M., Keyl A., Feussner I. Wax biosynthesis in response to danger: Its regulation upon abiotic and biotic stress. New Phytol. 2020;227:698–713. doi: 10.1111/nph.16571. - DOI - PubMed
    1. Paul S., Gable K., Beaudoin F., Cahoon E., Jaworski J., Napier J.A., Dunn T.M. Members of the Arabidopsis FAE1-like 3-ketoacyl-CoA synthase gene family substitute for the Elop proteins of Saccharomyces cerevisiae. J. Biol. Chem. 2006;281:9018–9029. doi: 10.1074/jbc.M507723200. - DOI - PubMed
    1. Funa N., Ohnishi Y., Ebizuka Y., Horinouchi S. Alteration of reaction and substrate specificity of a bacterial type III polyketide synthase by site-directed mutagenesis. Biochem. J. 2002;367:781–789. doi: 10.1042/bj20020953. - DOI - PMC - PubMed
    1. Sagar M., Pandey N., Qamar N., Singh B., Shukla A. Domain analysis of 3 Keto Acyl-CoA synthase for structural variations in Vitis vinifera and Oryza brachyantha using comparative modelling. Interdiscip. Sci. 2015;7:7–20. doi: 10.1007/s12539-013-0017-8. - DOI - PubMed

LinkOut - more resources