Research Articles

Genome-Wide Identification and Expression Profiling of the Laccase Gene Family in Tomato (Solanum lycopersicum) under Abiotic Stress and Hormonal Treatments

Sidra Ashraf, Farwa Yaqoob, Noor ul Ain & Sana Basharat

Received 8 Jun 2026, Published online: 10 Nov 2026

Published in Volume 1, Issue 2, 2026, pages e0013

Open access

Abstract

Laccase (LAC) is a class of multi-copper oxidases that plays an important role in plant lignin synthesis, cell wall formation, growth and development, and stress responses. However, systematic research on the tomato LAC gene family remains relatively limited. This study identified 24 members of the SlLAC gene family in the tomato genome and comprehensively analyzed their physicochemical properties, phylogenetic relationships, conserved domains, chromosome distribution, expression patterns, and miRNA regulation. Results showed that SlLAC proteins ranged in length from 484 to 614 aa and in molecular weight from 53.78 to 68.72 kDa; most members were basic and hydrophilic. The 24 SlLAC genes were unevenly distributed across 10 chromosomes, with chromosomes 5 and 6 containing the most members. Phylogenetic analysis divided the SlLAC family into several subgroups and showed high homology with Arabidopsis thaliana AtLAC proteins. Multiple sequence alignment results showed that all SlLAC proteins contained typical copper ion-binding conserved domains (L1–L4), indicating that they belong to a typical multi-copper oxidase family. Tissue expression analysis revealed that SlLAC genes exhibited significant spatiotemporal expression specificity in different tissues and fruit development stages. Among them, SlLAC23 was highly expressed in leaves, roots, and young fruits, while SlLAC22 was most significantly expressed in flowers. Stress treatment results showed that most SlLAC genes responded to salt, drought, and low-temperature stress to varying degrees, with some genes, such as SlLAC10, SlLAC11, and SlLAC22, showing significant induced expression under multiple stress conditions. Hormone treatment analysis further indicated that SlLAC genes exhibited complex dynamic expression patterns in response to plant hormones such as Eth, GA₃, IAA, SA, and JA. miRNA targeting prediction results showed that eight SlLAC genes could be targeted and regulated by sly-miR397, suggesting that the miR397-SlLAC module may be involved in the regulation of tomato lignin metabolism and stress response. In summary, this study systematically revealed the structural characteristics, evolutionary relationships, and expression patterns of the SlLAC gene family, providing an important theoretical basis for further research on the functions of SlLAC genes in tomato growth and development, fruit ripening, and stress adaptation.

Keywords

  • Tomato
  • Laccase
  • SlLAC
  • Phylogeny
  • Abiotic stress
  • Plant hormones
  • miR397
Views: 0Downloads: 0

References

  1. [1] M. B. Kaczmarek, N. Kwiatos, M. Szczęsna-Antczak, and S. Bielecki, "Laccases–enzymes with an unlimited potential." Biotechnology and Food Science, vol. 81, no. 1, pp. 41-70, 2017.
  2. [2] Y. Tobimatsu and M. Schuetz, "Lignin polymerization: how do plants manage the chemistry so well?"," Current opinion in biotechnology, vol. 56, pp. 75-81, 2019.
  3. [3] S. Berthet, N. Demont-Caulet, B. Pollet, P. Bidzinski, L. Cézard, P. Le Bris, N. Borrega, J. Hervé, E. Blondet, S. Balzergue, C. Lapierre, and L. Jouanin, "Disruption of LACCASE4 and 17 results in tissue-specific alterations to lignification of Arabidopsis thaliana stems," Plant Cell, vol. 23, pp. 1124-37, 2011.
  4. [4] Q. Zhao, J. Nakashima, F. Chen, Y. Yin, C. Fu, J. Yun, H. Shao, X. Wang, Z. Y. Wang, and R. A. Dixon, "Laccase is necessary and nonredundant with peroxidase for lignin polymerization during vascular development in Arabidopsis." Plant Cell, vol. 25, pp. 3976-3987, 2013.
  5. [5] L. Pourcel, J. M. Routaboul, L. Kerhoas, M. Caboche, L. Lepiniec, and I. Debeaujon, "TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat." Plant Cell, vol. 17, p. 2966–2980, 2005.
  6. [6] J. Zhu, H. Zhang, K. Huang, R. Guo, J. Zhao, H. Xie, J. Zhu, H. Gu, H. Chen, G. Li, and C. Wei, "Comprehensive analysis of the laccase gene family in tea plant highlights its roles in development and stress responses." BMC Plant Biology, vol. 23, no. 1, p. 129, 2023.
  7. [7] Y. Yu, Y. Xing, F. Liu, X. Zhang, X. Li, J. Zhang, and X. Sun, "The laccase gene family mediate multi-perspective trade-offs during tea plant (Camellia sinensis) development and defense processes," International journal of molecular sciences, vol. 22, no. 22, p. 12554, 2021.
  8. [8] X. Ping, T. Wang, N. Lin, F. Di, Y. Li, H. Jian, H. Wang, K. Lu, J. Li, X. Xu, and L. Liu, "Genome-wide identification of the LAC gene family and its expression analysis under stress in Brassica napus," Molecules, vol. 24, no. 10, p. 1985, 2019.
  9. [9] B. C. McCaig, R. B. Meagher, and J. F. Dean, "Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana." Planta, vol. 221, no. 5, pp. 619-636, 2005.
  10. [10] Q. Liu, L. Luo, X. Wang, Z. Shen, and L. Zheng, "Comprehensive analysis of rice laccase gene (OsLAC) family and ectopic expression of OsLAC10 enhances tolerance to copper stress in Arabidopsis." International Journal of Molecular Sciences,, vol. 18, no. 2, p. 209, 2017.
  11. [11] Q. Wang, G. Li, K. Zheng, X. Zhu, J. Ma, D. Wang, K. Tang, X. Feng, J. Leng, H. Yu, and S. Yang, "The soybean laccase gene family: Evolution and possible roles in plant defense and stem strength selection." Genes, vol. 10, no. 9, p. 701, 2019.
  12. [12] T. Cheng, C. Ren, J. Xu, H. Wang, B. Wen, Q. Zhao, W. Zhang, G. Yu, and Y. Zhang, "Genome-wide analysis of the common bean (Phaseolus vulgaris) laccase gene family and its functions in response to abiotic stress," BMC Plant Biology, vol. 24, no. 1, p. 688, 2024.
  13. [13] X. Xu, Y. Zhou, B. Wang, L. Ding, Y. Wang, L. Luo, Y. Zhang, and W. Kong, "Genome-wide identification and characterization of laccase gene family in Citrus sinensis." Gene, vol. 689, pp. 114-123, 2019.
  14. [14] S. Lu, Q. Li, H. Wei, M. J. Chang, S. Tunlaya-Anukit, H. Kim, J. Liu, J. Song, Y. H. Sun, L. Yuan, and T. F. Yeh, "Ptr-miR397a is a negative regulator of laccase genes affecting lignin content in Populus trichocarpa," Proceedings of the National Academy of Sciences, vol. 110, no. 26, pp. 10848-10853, 2013.
  15. [15] C. Y. Wang, S. Zhang, Y. Yu, Y. C. Luo, Q. Liu, C. Ju, Y. C. Zhang, L. H. Qu, W. J. Lucas, X. Wang, and Y. Q. Chen, " MiR397b regulates both lignin content and seed number in Arabidopsis via modulating a laccase involved in lignin biosynthesis." Plant Biotechnology Journal, vol. 12, pp. 1132-1142, 2014.
  16. [16] H. Khandal, A. P. Singh, and D. Chattopadhyay, " MicroRNA397bLACCASE2 module regulates root lignification under water- and phosphate deficiency," Plant Physiology, vol. 182, pp. 1387-1403, 2020.
  17. [17] 100 Tomato Genome Sequencing Consortium, S. Aflitos, E. Schijlen, H. de Jong, D. de Ridder, S. Smit, R. Finkers, J. Wang, G. Zhang, N. Li, and L. Mao, "Exploring genetic variation in the tomato (Solanum section Lycopersicon) clade by whole‐genome sequencing," The Plant Journal, vol. 80, no. 1, pp. 136-148, 2014.
  18. [18] S. R. Eddy, “Accelerated profile HMM searches,” PLoS Computational Biology, vol. 7, no. 10, e1002195, 2011. doi:10.1371/journal.pcbi.1002195.
  19. [19] I. Letunic, S. Khedkar, and P. Bork, “SMART: recent updates, new developments and status in 2020,” Nucleic Acids Research, vol. 49, no. D1, pp. D458–D460, 2021. doi:10.1093/nar/gkaa937.
  20. [20] S. Lu et al., “CDD/SPARCLE: the conserved domain database in 2020,” Nucleic Acids Research, vol. 48, no. D1, pp. D265–D268, 2020. doi:10.1093/nar/gkz991.
  21. [21] E. Gasteiger, C. Hoogland, A. Gattiker, S. Duvaud, M. R. Wilkins, R. D. Appel, and A. Bairoch, “Protein identification and analysis tools on the ExPASy server,” in The Proteomics Protocols Handbook, J. M. Walker, Ed. Humana Press, 2005, pp. 571–607. doi:10.1385/1-59259-890-0:571.
  22. [22] C. Chen, Y. Wu, J. Li, X. Wang, Z. Zeng, J. Xu, Y. Liu, J. Feng, H. Chen, Y. He, and R. Xia, "TBtools-II: A “one for all, all for one” bioinformatics platform for biological big-data mining," Molecular plant, vol. 16, no. 11, pp. 1733-1742., 2023.
  23. [23] P. Horton, K. J. Park, T. Obayashi, N. Fujita, H. Harada, C. J. Adams-Collier, and K. Nakai, "WoLF PSORT: protein localization predictor." Nucleic acids research,, vol. 35, no. (suppl_2), pp. W585-W587, 2007.
  24. [24] B. Hu, J. Jin, A. Y. Guo, H. Zhang, J. Luo, and G. Gao, “GSDS 2.0: an upgraded gene feature visualization server,” Bioinformatics, vol. 31, no. 8, pp. 1296–1297, 2015. doi:10.1093/bioinformatics/btu817.
  25. [25] J. D. Thompson, D. G. Higgins, and T. J. Gibson, “CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice,” Nucleic Acids Research, vol. 22, no. 22, pp. 4673–4680, 1994. doi:10.1093/nar/22.22.4673.
  26. [26] S. Kumar, G. Stecher, and K. Tamura, “MEGA7: Molecular Evolutionary Genetics Analysis version 7.0 for bigger datasets,” Molecular Biology and Evolution, vol. 33, no. 7, pp. 1870–1874, 2016. doi:10.1093/molbev/msw054.
  27. [27] P. Gouet, X. Robert, and E. Courcelle, “ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins,” Nucleic Acids Research, vol. 31, no. 13, pp. 3320–3323, 2003. doi:10.1093/nar/gkg556.
  28. [28] X. Dai, Z. Zhuang, and P. X. Zhao, “psRNATarget: a plant small RNA target analysis server (2017 release),” Nucleic Acids Research, vol. 46, no. W1, pp. W49–W54, 2018. doi:10.1093/nar/gky316.
  29. [29] K. J. Livak and T. D. Schmittgen, “Analysis of relative gene expression data using real-time quantitative PCR and the 2⁻ΔΔCT method,” Methods, vol. 25, no. 4, pp. 402–408, 2001. doi:10.1006/meth.2001.1262.
  30. [30] S. A. Bustin et al., “The MIQE guidelines: minimum information for publication of quantitative real-time PCR experiments,” Clinical Chemistry, vol. 55, no. 4, pp. 611–622, 2009. doi:10.1373/clinchem.2008.112797.
  31. [31] P. J. Hoegger, S. Kilaru, T. Y. James, J. R. Thacker, and U. Kües, "Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences." The FEBS journal, vol. 273, no. 10, pp. 2308-2326, 2006.
  32. [32] P. V. Turlapati, K. W. Kim, L. B. Davin, and N. G. Lewis, "The laccase multigene family in Arabidopsis thaliana: towards addressing the mystery of their gene function (s)," Planta, vol. 233, no. 3, pp. 439-470, 2011.
  33. [33] J. Wang, J. Feng, W. Jia, S. Chang, S. Li, and Y. Li, "Lignin engineering through laccase modification: A promising field for energy plant improvement," Biotechnology Biofuels, vol. 8, p. 145, 2015.[34] R. Sterjiades, J. F. Dean, G. Gamble, D. S. Himmelsbach, and K. E. L. Eriksson, "Extracellular laccases and peroxidases from sycamore maple (Acer pseudoplatanus) cell-suspension cultures: reactions with monolignols and lignin model compounds." Planta, vol. 190, no. 1, pp. 75-87, 1993.

Metrics

Article views
0
Downloads
0

Licensing

This article is published under CC BY 4.0.

How to cite

Ashraf, S., Yaqoob, F., Ain, N. U., & Basharat, S. (2026). Genome-Wide Identification and Expression Profiling of the Laccase Gene Family in Tomato (Solanum lycopersicum) under Abiotic Stress and Hormonal Treatments. Plant Science Horizons, 1(2), e0013. https://doi.org/10.66835/psh.2026.e0013

How to Cite

Ashraf, S., Yaqoob, F., Ain, N. ul, & Basharat, S. (2026). Genome-Wide Identification and Expression Profiling of the Laccase Gene Family in Tomato (Solanum lycopersicum) under Abiotic Stress and Hormonal Treatments. Plant Science Horizons, 1(2), e0013. https://doi.org/10.66835/psh.2026.e0013

Similar Articles

You may also start an advanced similarity search for this article.

Most read articles by the same author(s)