Abstract
Phytohormones are the main regulatory molecules of core signalling networks associated with plant life cycle regulation. Manipulation of hormone signalling cascade enables the control over physiological traits of plant, which has major applications in field of agriculture and food sustainability. Hence, stable analogues of these hormones are long sought after and many of them are currently known, but the quest for more effective, stable and economically viable analogues is still going on. This search has been further strengthened by the identification of the components of signalling cascade such as receptors, downstream cascade members and transcription factors. Furthermore, many proteins of phytohormone cascades are available in crystallized forms. Such crystallized structures can provide the basis for identification of novel interacting compounds using in silico approach. Plenty of computational tools and bioinformatics software are now available that can aid in this process. Here, the metadata of all the major phytohormone signalling cascades are presented along with discussion on major protein–ligand interactions and protein components that may act as a potential target for manipulation of phytohormone signalling cascade. Furthermore, structural aspects of phytohormones and their known analogues are also discussed that can provide the basis for the synthesis of novel analogues.
Similar content being viewed by others
References
Ben-Ari, G. (2012). The ABA signal transduction mechanism in commercial crops: Learning from Arabidopsis. Plant Cell Reports, 31, 1357–1369.
Schwechheimer, C., & Willige, B. C. (2009). Shedding light on gibberellic acid signalling. Current Opinion in Plant Biology, 12, 57–62.
Fu, X., & Harberd, N. P. (2003). Auxin promotes Arabidopsis root growth by modulating gibberellin response. Nature, 421, 740–743. https://doi.org/10.1038/nature01387
Planas-Riverola, A., Gupta, A., Betegón-Putze, I., Bosch, N., Ibañes, M., & Caño-Delgado, A. I. (2019). Brassinosteroid signaling in plant development and adaptation to stress. Development, 146(5), dev51894.
Prerostova, S., Dobrev, P. I., Gaudinova, A., et al. (2018). Cytokinins: Their impact on molecular and growth responses to drought stress and recovery in arabidopsis. Frontiers in Plant Science. https://doi.org/10.3389/fpls.2018.00655
Wasternack, C., & Song, S. (2017). Jasmonates: Biosynthesis, metabolism, and signaling by proteins activating and repressing transcription. Journal of Experimental Botany, 68, 1303–1321.
Park, S. W., Kaimoyo, E., Kumar, D., et al. (2007). Methyl salicylate is a critical mobile signal for plant systemic acquired resistance. Science (-80), 318, 113–116. https://doi.org/10.1126/science.1147113
Akiyama, K., Matsuzaki, K. I., & Hayashi, H. (2005). Plant sesquiterpenes induce hyphal branching in arbuscular mycorrhizal fungi. Nature, 435, 824–827. https://doi.org/10.1038/nature03608
Iqbal, N., Khan, N. A., Ferrante, A., et al. (2017). Ethylene role in plant growth, development and senescence: Interaction with other phytohormones. Frontiers in Plant Science, 8, 475. https://doi.org/10.3389/fpls.2017.00475
Larrieu, A., & Vernoux, T. (2015). Comparison of plant hormone signalling systems. Essays in Biochemistry, 58, 165–181. https://doi.org/10.1042/BSE0580165
Díaz, K., Espinoza, L., Carvajal, R., et al. (2020). Biological activities and molecular docking of brassinosteroids 24-norcholane type analogs. International Journal of Molecular Sciences, 21, 1832. https://doi.org/10.3390/ijms21051832
Park, S. Y., Fung, P., Nishimura, N., et al. (2009). Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins. Science (-80), 324, 1068–1071. https://doi.org/10.1126/science.1173041
Baitha, A., Upadhyay, M., Gopinathan, A., et al. (2019). Synthesis, characterization, and docking studies of novel cyanopyridone analogs with serotonin 5-HT1B receptor agonists. Synthetic Communications, 49, 844–851. https://doi.org/10.1080/00397911.2019.1575422
Pagadala, N. S., Syed, K., & Tuszynski, J. (2017). Software for molecular docking: A review. Biophysical Reviews, 9, 91–102.
Rajagopalan, N., Nelson, K. M., Douglas, A. F., et al. (2016). Abscisic acid analogues that act as universal or selective antagonists of phytohormone receptors. Biochemistry, 55, 5155–5164. https://doi.org/10.1021/acs.biochem.6b00605
Hsu, P. K., Dubeaux, G., Takahashi, Y., & Schroeder, J. I. (2021). Signaling mechanisms in abscisic acid-mediated stomatal closure. The Plant Journal, 105, 307–321. https://doi.org/10.1111/tpj.15067
Soon, F. F., Ng, L. M., Zhou, X. E., et al. (2012). Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases. Science (-80), 335, 85–88. https://doi.org/10.1126/science.1215106
Takahashi, Y., Zhang, J., Hsu, P. K., et al. (2020). MAP3Kinase-dependent SnRK2-kinase activation is required for abscisic acid signal transduction and rapid osmotic stress response. Nature Communications, 11, 1–12. https://doi.org/10.1038/s41467-019-13875-y
Nishimura, N., Hitomi, K., Arvai, A. S., et al. (2009). Structural mechanism of abscisic acid binding and signaling by dimeric PYR1. Science (-80), 326, 1373–1379. https://doi.org/10.1126/science.1181829
Dupeux, F., Antoni, R., Betz, K., et al. (2011). Modulation of abscisic acid signaling in vivo by an engineered receptor-insensitive protein phosphatase type 2C allele. Plant Physiology, 156, 106–116. https://doi.org/10.1104/pp.110.170894
Takeuchi, J., Okamoto, M., Akiyama, T., et al. (2014). Designed abscisic acid analogs as antagonists of PYL-PP2C receptor interactions. Nature Chemical Biology, 10, 477–482. https://doi.org/10.1038/nchembio.1524
Strnad, M. (1997). The aromatic cytokinins. Physiologia Plantarum, 101, 674–688. https://doi.org/10.1111/j.1399-3054.1997.tb01052.x
Hönig, M., Plíhalová, L., Husičková, A., Nisler, J., & Doležal, K. (2018). Role of cytokinins in senescence, antioxidant defence and photosynthesis. International Journal of Molecular Sciences, 19(12), 4045.
Gamas, P., Brault, M., Jardinaud, M. F., & Frugier, F. (2017). Cytokinins in symbiotic nodulation: When, where, what for? Trends in Plant Science, 22, 792–802.
Akhtar, S. S., Mekureyaw, M. F., Pandey, C., & Roitsch, T. (2020). Role of cytokinins for interactions of plants with microbial pathogens and pest insects. Frontiers in Plant Science, 10, 1777.
Chang, J., Li, X., Fu, W., et al. (2019). Asymmetric distribution of cytokinins determines root hydrotropism in Arabidopsis thaliana. Cell Research, 29, 984–993. https://doi.org/10.1038/s41422-019-0239-3
Hothorn, M., Dabi, T., & Chory, J. (2011). Structural basis for cytokinin recognition by Arabidopsis thaliana histidine kinase 4. Nature Chemical Biology, 7, 766–768. https://doi.org/10.1038/nchembio.667
Bauer, J., Reiss, K., Veerabagu, M., et al. (2013). Structure-function analysis of arabidopsis thaliana histidine kinase AHK5 bound to its cognate phosphotransfer protein AHP1. Molecular Plant, 6, 959–970. https://doi.org/10.1093/mp/sss126
Hosoda, K., Imamura, A., Katoh, E., et al. (2002). Molecular structure of the GARP family of plant myb-related DNA binding motifs of the Arabidopsis response regulators. The Plant Cell, 14, 2015–2029. https://doi.org/10.1105/tpc.002733
Suzuki, T., Miwa, K., Ishikawa, K., et al. (2001). The Arabidopsis sensor His-kinase, AHK4, can respond to cytokinins. Plant and Cell Physiology, 42, 107–113. https://doi.org/10.1093/pcp/pce037
Hwang, I., & Sheen, J. (2001). Two-component circuitry in Arabidopsis cytokinin signal transduction. Nature, 413, 383–389. https://doi.org/10.1038/35096500
Hutchison, C. E., Li, J., Argueso, C., et al. (2006). The Arabidopsis histidine phosphotransfer proteins are redundant positive regulators of cytokinin signaling. The Plant Cell, 18, 3073–3087. https://doi.org/10.1105/tpc.106.045674
D’Agostino, I. B., Deruère, J., & Kieber, J. J. (2000). Characterization of the response of the Arabidopsis response regulator gene family to cytokinin. Plant Physiology, 124, 1706–1717. https://doi.org/10.1104/pp.124.4.1706
Bakshi, A., Shemansky, J. M., Chang, C., & Binder, B. M. (2015). History of research on the plant hormone ethylene. Journal of Plant Growth Regulation, 34, 809–827.
Abiri, R., Shaharuddin, N. A., Maziah, M., et al. (2017). Role of ethylene and the APETALA 2/ethylene response factor superfamily in rice under various abiotic and biotic stress conditions. Environmental and Experimental Botany, 134, 33–44.
Klay, I., Gouia, S., Liu, M., et al. (2018). Ethylene Response Factors (ERF) are differentially regulated by different abiotic stress types in tomato plants. Plant Science, 274, 137–145. https://doi.org/10.1016/j.plantsci.2018.05.023
Ansari, M. W., & Tuteja, N. (2013). Stress-induced ethylene in postharvest losses of perishable products. Stewart Postharvest Review, 9, 1–5. https://doi.org/10.2212/spr.2013.4.4
Chang, C., Kwok, S. F., Bleecker, A. B., & Meyerowitz, E. M. (1993). Arabidopsis ethylene-response gene ETR1: Similarity of product to two-component regulators. Science (-80), 262, 539–544. https://doi.org/10.1126/science.8211181
Hua, J., Chang, C., Sun, Q., & Meyerowitz, E. M. (1995). Ethylene insensitivity conferred by Arabidopsis EPS gene. Science (-80), 269, 1712–1714. https://doi.org/10.1126/science.7569898
Hua, J., Sakai, H., Nourizadeh, S., et al. (1998). EIN4 and ERS2 are members of the putative ethylene receptor gene family in arabidopsis. The Plant Cell, 10, 1321–1332. https://doi.org/10.1105/tpc.10.8.1321
Sakai, H., Hua, J., Chen, Q. G., et al. (1998). ETR2 is an ETR1-like gene involved in ethylene signaling in Arabidopsis. Proceedings of the National Academy of Sciences of the United States of America, 95, 5812–5817. https://doi.org/10.1073/pnas.95.10.5812
Mayerhofer, H., Panneerselvam, S., Kaljunen, H., et al. (2015). Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). Journal of Biological Chemistry, 290, 2644–2658. https://doi.org/10.1074/jbc.M114.587667
Bisson, M. M. A., & Groth, G. (2010). New insight in ethylene signaling: Autokinase activity of ETR1 modulates the interaction of receptors and EIN2. Molecular Plant, 3, 882–889. https://doi.org/10.1093/mp/ssq036
Kieber, J. J., Rothenberg, M., Roman, G., et al. (1993). CTR1, a negative regulator of the ethylene response pathway in arabidopsis, encodes a member of the Raf family of protein kinases. Cell, 72, 427–441. https://doi.org/10.1016/0092-8674(93)90119-B
Binder, B. M. (2020). Ethylene signaling in plants. Journal of Biological Chemistry, 295, 7710–7725. https://doi.org/10.1074/jbc.REV120.010854
Zimmermann, M., Clarke, O., Gulbis, J. M., et al. (2009). Metal binding affinities of Arabidopsis zinc and copper transporters: Selectivities match the relative, but not the absolute, affinities of their amino-terminal domains. Biochemistry, 48, 11640–11654. https://doi.org/10.1021/bi901573b
Rodríguez, F. I., Esch, J. J., Hall, A. E., et al. (1999). A copper cofactor for the ethylene receptor ETR1 from Arabidopsis. Science (-80), 283, 996–998. https://doi.org/10.1126/science.283.5404.996
Mayerhofer, H., Panneerselvam, S., & Mueller-Dieckmann, J. (2012). Protein kinase domain of CTR1 from Arabidopsis thaliana promotes ethylene receptor cross talk. Journal of Molecular Biology, 415, 768–779. https://doi.org/10.1016/j.jmb.2011.11.046
Allen, M. D., Yamasaki, K., Ohme-Takagi, M., et al. (1998). A novel mode of DNA recognition by a β-sheet revealed by the solution structure of the GCC-box binding domain in complex with DNA. EMBO Journal, 17, 5484–5496. https://doi.org/10.1093/emboj/17.18.5484
Yamasaki, K., Kigawa, T., Inoue, M., et al. (2005). Solution structure of the major DNA-binding domain of Arabidopsis thaliana ethylene-insensitive3-like3. Journal of Molecular Biology, 348, 253–264. https://doi.org/10.1016/j.jmb.2005.02.065
Song, J., Zhu, C., Zhang, X., et al. (2015). Biochemical and structural insights into the mechanism of DNA recognition by arabidopsis ETHYLENE INSENSITIVE3. PLoS ONE. https://doi.org/10.1371/journal.pone.0137439
Sisler, E. C., Dupille, E., & Serek, M. (1996). Effect of 1-methylcyclopropene and methylenecyclopropane on ethylene binding and ethylene action on cut carnations. Plant Growth Regulation, 18, 79–86. https://doi.org/10.1007/bf00028491
Li, W., Lacey, R. F., Ye, Y., et al. (2017). Triplin, a small molecule, reveals copper ion transport in ethylene signaling from ATX1 to RAN1. PLoS Genetics. https://doi.org/10.1371/journal.pgen.1006703
Pirrung, M. C., Bleecker, A. B., Inoue, Y., et al. (2008). Ethylene receptor antagonists: Strained alkenes are necessary but not sufficient. Chemistry & Biology, 15, 313–321. https://doi.org/10.1016/j.chembiol.2008.02.018
Clause, S. D., & Sasse, J. M. (1998). Brassinosteroids: Essential regulators of plant growth and development. Annual Review of Plant Biology, 49, 427–451. https://doi.org/10.1146/annurev.arplant.49.1.427
Kang, Y. H., Breda, A., & Hardtke, C. S. (2017). Brassinosteroid signaling directs formative cell divisions and protophloem differentiation in Arabidopsis root meristems. Dev, 144, 272–280. https://doi.org/10.1242/dev.145623
Yamaguchi, M., Goué, N., Igarashi, H., et al. (2010). VASCULAR-RELATED NAC-DOMAIN6 and VASCULAR-RELATED NAC-DOMAIN7 effectively induce transdifferentiation into xylem vessel elements under control of an induction system. Plant Physiology, 153, 906–914. https://doi.org/10.1104/pp.110.154013
De Bruyne, L., Höfte, M., & De Vleesschauwer, D. (2014). Connecting growth and defense: The emerging roles of brassinosteroids and gibberellins in plant innate immunity. Molecular Plant, 7, 943–959.
Ye, H., Liu, S., Tang, B., et al. (2017). RD26 mediates crosstalk between drought and brassinosteroid signalling pathways. Nature Communications, 8, 1–13. https://doi.org/10.1038/ncomms14573
Tunc-Ozdemir, M., & Jones, A. M. (2017). BRL3 and AtRGS1 cooperate to fine tune growth inhibition and ROS activation. PLoS ONE, 12, e0177400. https://doi.org/10.1371/journal.pone.0177400
Fàbregas, N., Lozano-Elena, F., Blasco-Escámez, D., et al. (2018). Overexpression of the vascular brassinosteroid receptor BRL3 confers drought resistance without penalizing plant growth. Nature Communications, 9, 1–13. https://doi.org/10.1038/s41467-018-06861-3
Chai, J., Han, Z., & Sun, Y. (2013). Structural insight into BL-induced activation of the BRI1-BAK1complex.
Wang, Z. X., Wang, J., Jiang, J., et al. (2014). Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1. Cell Research, 24, 1328–1341. https://doi.org/10.1038/cr.2014.132
Nosaki, S., Miyakawa, T., Xu, Y., et al. (2018). Structural basis for brassinosteroid response by BIL1/BZR1. Nature Plants, 4, 771–776. https://doi.org/10.1038/s41477-018-0255-1
She, J., Han, Z., Kim, T. W., et al. (2011). Structural insight into brassinosteroid perception by BRI1. Nature, 474, 472–477. https://doi.org/10.1038/nature10178
She, J., Han, Z., Zhou, B., & Chai, J. (2013). Structural basis for differential recognition of brassinolide by its receptors. Protein & Cell, 4, 475–482. https://doi.org/10.1007/s13238-013-3027-8
Liu, J., Zhang, D., Sun, X., et al. (2017). Structure-activity relationship of brassinosteroids and their agricultural practical usages. Steroids, 124, 1–17.
Ali, B., Hayat, S., Hasan, S. A., & Ahmad, A. (2006). Effect of root applied 28-homobrassinolide on the performance of Lycopersicon esculentum. Scientia Horticulturae (Amsterdam), 110, 267–273. https://doi.org/10.1016/j.scienta.2006.07.015
Serna, M., Hernández, F., Coll, F., et al. (2012). Brassinosteroid analogues effects on the yield and quality parameters of greenhouse-grown pepper (Capsicum annuum L.). Plant Growth Regulation, 68, 333–342. https://doi.org/10.1007/s10725-012-9718-y
Sato, A., Sasaki, S., Matsuzaki, J., & Yamamoto, K. T. (2014). Light-dependent gravitropism and negative phototropism of inflorescence stems in a dominant Aux/IAA mutant of Arabidopsis thaliana, axr2. Journal of Plant Research, 127, 627–639. https://doi.org/10.1007/s10265-014-0643-1
Quintana-Escobar, A. O., Nic-Can, G. I., Galaz Avalos, R. M., et al. (2019). Transcriptome analysis of the induction of somatic embryogenesis in Coffea canephora and the participation of ARF and Aux/IAA genes. PeerJ, 2019, e7752. https://doi.org/10.7717/peerj.7752
Salazar-Iribe, A., & De-la-Peña, C. (2020). Auxins, the hidden player in chloroplast development. Plant Cell Reports, 39, 1595–1608.
Tan, X., Calderon-Villalobos, L. I. A., Sharon, M., et al. (2007). Mechanism of auxin perception by the TIR1 ubiquitin ligase. Nature, 446, 640–645. https://doi.org/10.1038/nature05731
Kim, Y., Park, C., Cha, S., et al. (2020). Determinants of PB1 domain interactions in Auxin response factor ARF5 and repressor IAA17. Journal of Molecular Biology, 432, 4010–4022. https://doi.org/10.1016/j.jmb.2020.04.007
Freire-Rios, A., Tanaka, K., Crespo, I., et al. (2020). Architecture of DNA elements mediating ARF transcription factor binding and auxin-responsive gene expression in Arabidopsis. Proceedings of the National Academy of Sciences of the United States of America, 117, 24557–24566. https://doi.org/10.1073/pnas.2009554117
Lee, S., Sundaram, S., Armitage, L., et al. (2014). Defining binding efficiency and specificity of auxins for SCF TIR1/AFB-Aux/IAA Co-receptor complex formation. ACS Chemical Biology, 9, 673–682. https://doi.org/10.1021/cb400618m
Uzunova, V. V., Quareshy, M., Del Genio, C. I., & Napier, R. M. (2016). Tomographic docking suggests the mechanism of auxin receptor TIR1 selectivity. Open Biology. https://doi.org/10.1098/rsob.160139
Tyler, L., Thomas, S. G., Hu, J., et al. (2004). Della proteins and gibberellin-regulated seed germination and floral development in Arabidopsis. Plant Physiology, 135, 1008–1019. https://doi.org/10.1104/pp.104.039578
Penfield, S., Gilday, A. D., Halliday, K. J., & Graham, I. A. (2006). DELLA-mediated cotyledon expansion breaks coat-imposed seed dormancy. Current Biology, 16, 2366–2370. https://doi.org/10.1016/j.cub.2006.10.057
Achard, P., Gusti, A., Cheminant, S., et al. (2009). Gibberellin signaling controls cell proliferation rate in arabidopsis. Current Biology, 19, 1188–1193. https://doi.org/10.1016/j.cub.2009.05.059
Djakovic-Petrovic, T., De, W. M., Voesenek, L. A. C. J., & Pierik, R. (2007). DELLA protein function in growth responses to canopy signals. The Plant Journal, 51, 117–126. https://doi.org/10.1111/j.1365-313X.2007.03122.x
Jiang, C., Gao, X., Liao, L., et al. (2007). Phosphate starvation root architecture and anthocyanin accumulation responses are modulated by the gibberellin-DELLA signaling pathway in Arabidopsis. Plant Physiology, 145, 1460–1470. https://doi.org/10.1104/pp.107.103788
Achard, P., Baghour, M., Chapple, A., et al. (2007). The plant stress hormone ethylene controls floral transition via DELLA-dependent regulation of floral meristem-identity genes. Proceedings of the National Academy of Sciences of the United States of America, 104, 6484–6489. https://doi.org/10.1073/pnas.0610717104
MacMillan, J. (2001). Occurrence of gibberellins in vascular plants, fungi, and bacteria. Journal of Plant Growth Regulation, 20, 387–442. https://doi.org/10.1007/s003440010038
Ueguchi-Tanaka, M., & Matsuoka, M. (2010). The perception of gibberellins: Clues from receptor structure. Current Opinion in Plant Biology, 13, 503–508.
Murase, K., Hirano, Y., Sun, T. P., & Hakoshima, T. (2008). Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. Nature, 456, 459–463. https://doi.org/10.1038/nature07519
Fonouni-Farde, C., Diet, A., & Frugier, F. (2016). Root development and endosymbioses: DELLAs lead the orchestra. Trends in Plant Science, 21, 898–900.
Locascio, A., Blázquez, M. A., & Alabadí, D. (2013). Dynamic regulation of cortical microtubule organization through prefoldin-DELLA interaction. Current Biology, 23, 804–809. https://doi.org/10.1016/j.cub.2013.03.053
Fan, D., Ran, L., Hu, J., et al. (2020). miR319a/TCP module and DELLA protein regulate trichome initiation synergistically and improve insect defenses in Populus tomentosa. New Phytologist, 227, 867–883. https://doi.org/10.1111/nph.16585
Richter, R., Behringer, C., Müller, I. K., & Schwechheimer, C. (2010). The GATA-type transcription factors GNC and GNL/CGA1 repress gibberellin signaling downstream from DELLA proteins and phytochrome-interacting factors. Genes & Development, 24, 2093–2104. https://doi.org/10.1101/gad.594910
Zentella, R., Zhang, Z. L., Park, M., et al. (2007). Global analysis of DELLA direct targets in early gibberellin signaling in Arabidopsis. The Plant Cell, 19, 3037–3057. https://doi.org/10.1105/tpc.107.054999
Lau, O. S., & Deng, X. W. (2010). Plant hormone signaling lightens up: Integrators of light and hormones. Current Opinion in Plant Biology, 13, 571–577.
Wild, M., Davière, J. M., Cheminant, S., et al. (2012). The Arabidopsis DELLA RGA-LIKE3 is a direct target of MYC2 and modulates jasmonate signaling responses. The Plant Cell, 24, 3307–3319. https://doi.org/10.1105/tpc.112.101428
Jing, Y., Guo, Q., Zha, P., & Lin, R. (2019). The chromatin-remodelling factor PICKLE interacts with CONSTANS to promote flowering in Arabidopsis. Plant, Cell and Environment, 42, 2495–2507. https://doi.org/10.1111/pce.13557
Itoh, H., Ueguchi-Tanaka, M., Sato, Y., et al. (2002). The gibberellin signaling pathway is regulated by the appearance and disappearance of slender rice1 in nuclei. The Plant Cell, 14, 57–70. https://doi.org/10.1105/tpc.010319
Mander, L. N., Sherburn, M., Camp, D., et al. (1998). Effects of d-ring modified gibberellins on flowering and growth in Lolium temulentum. Phytochemistry, 49, 2195–2206. https://doi.org/10.1016/S0031-9422(98)00310-0
Bergner, C., Lischewski, M., Adam, G., & Sembdner, G. (1982). Biological activity of gibberellin analogues. Planta, 155, 231–237. https://doi.org/10.1007/BF00392721
Tian, H., Xu, Y., Liu, S., et al. (2017). Synthesis of gibberellic acid derivatives and their effects on plant growth. Molecules. https://doi.org/10.3390/molecules22050694
Wasternack, C., & Hause, B. (2013). Jasmonates: Biosynthesis, perception, signal transduction and action in plant stress response, growth and development. An update to the 2007 review in Annals of Botany. Annals of Botany, 111, 1021–1058.
Campos, M. L., Kang, J. H., & Howe, G. A. (2014). Jasmonate-triggered plant immunity. Journal of Chemical Ecology, 40, 657–675. https://doi.org/10.1007/s10886-014-0468-3
Ruan, J., Zhou, Y., Zhou, M., et al. (2019). Jasmonic acid signaling pathway in plants. International Journal of Molecular Sciences, 20, 2479.
Zhang, F., Ke, J., Zhang, L., et al. (2017). Structural insights into alternative splicing-mediated desensitization of jasmonate signaling. Proceedings of the National Academy of Sciences of the United States of America, 114, 1720–1725. https://doi.org/10.1073/pnas.1616938114
Zhang, F., Yao, J., Ke, J., et al. (2015). Structural basis of JAZ repression of MYC transcription factors in jasmonate signalling. Nature, 525, 269–273. https://doi.org/10.1038/nature14661
Martin-Arevalillo, R., Nanao, M. H., Larrieu, A., et al. (2017). Structure of the Arabidopsis TOPLESS corepressor provides insight into the evolution of transcriptional repression. Proceedings of the National Academy of Sciences of the United States of America, 114, 8107–8112. https://doi.org/10.1073/pnas.1703054114
Xie, D. X., Feys, B. F., James, S., et al. (1998). COI1: An Arabidopsis gene required for jasmonate-regulated defense and fertility. Science (-80), 280, 1091–1094. https://doi.org/10.1126/science.280.5366.1091
Yang, J., Duan, G., Li, C., et al. (2019). The crosstalks between jasmonic acid and other plant hormone signaling highlight the involvement of jasmonic acid as a core component in plant response to biotic and abiotic stresses. Frontiers in Plant Science, 10, 1349.
Sheard, L. B., Tan, X., Mao, H., et al. (2010). Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-receptor. Nature, 468, 400–407. https://doi.org/10.1038/nature09430
Sloan, J., Hakenjos, J. P., Gebert, M., et al. (2020). Structural basis for the complex DNA binding behavior of the plant stem cell regulator WUSCHEL. Nature Communications. https://doi.org/10.1038/s41467-020-16024-y
Ke, J., Ma, H., Gu, X., et al. (2015). Structural basis for recognition of diverse transcriptional repressors by the TOPLESS family of corepressors. Science Advances. https://doi.org/10.1126/sciadv.1500107
Honda, I., Seto, H., Turuspekov, Y., et al. (2006). Inhibitory effects of jasmonic acid and its analogues on barley (Hordeum vulgare L.) anther extrusion. Plant Growth Regulation, 48, 201–206. https://doi.org/10.1007/s10725-006-0003-9
Pathak, R. K., Baunthiyal, M., Shukla, R., et al. (2017). In silico identification of mimicking molecules as defense inducers triggering jasmonic acid mediated immunity against alternaria blight disease in brassica species. Frontiers in Plant Science, 8, 609. https://doi.org/10.3389/fpls.2017.00609
Cook, C. E., Whichard, L. P., Turner, B., et al. (1966). Germination of witchweed (striga lutea lour.): Isolation and properties of a potent stimulant. Science (-80), 154, 1189–1190. https://doi.org/10.1126/science.154.3753.1189
Xie, X. (2016). Structural diversity of strigolactones and their distribution in the plant kingdom. Journal of Pesticide Science, 41, 175–180. https://doi.org/10.1584/jpestics.J16-02
Bürger, M., & Chory, J. (2020). The many models of strigolactone signaling. Trends in Plant Science, 25, 395–405.
Yoneyama, K., Xie, X., Kusumoto, D., et al. (2007). Nitrogen deficiency as well as phosphorus deficiency in sorghum promotes the production and exudation of 5-deoxystrigol, the host recognition signal for arbuscular mycorrhizal fungi and root parasites. Planta, 227, 125–132. https://doi.org/10.1007/s00425-007-0600-5
Zhao, L. H., Zhou, X. E., Yi, W., et al. (2015). Destabilization of strigolactone receptor DWARF14 by binding of ligand and E3-ligase signaling effector DWARF3. Cell Research, 25, 1219–1236. https://doi.org/10.1038/cr.2015.122
Yao, R., Ming, Z., Yan, L., et al. (2016). DWARF14 is a non-canonical hormone receptor for strigolactone. Nature, 536, 469–473. https://doi.org/10.1038/nature19073
Abe, S., Sado, A., Tanaka, K., et al. (2014). Carlactone is converted to carlactonoic acid by MAX1 in Arabidopsis and its methyl ester can directly interact with AtD14 in vitro. Proceedings of the National Academy of Sciences of the United States of America, 111, 18084–18089. https://doi.org/10.1073/pnas.1410801111
Ueno, K., Furumoto, T., Umeda, S., et al. (2014). Heliolactone, a non-sesquiterpene lactone germination stimulant for root parasitic weeds from sunflower. Phytochemistry, 108, 122–128. https://doi.org/10.1016/j.phytochem.2014.09.018
Charnikhova, T. V., Gaus, K., Lumbroso, A., et al. (2017). Zealactones. Novel natural strigolactones from maize. Phytochemistry, 137, 123–131. https://doi.org/10.1016/j.phytochem.2017.02.010
Il, K. H., Kisugi, T., Khetkam, P., et al. (2014). Avenaol, a germination stimulant for root parasitic plants from Avena strigosa. Phytochemistry, 103, 85–88. https://doi.org/10.1016/j.phytochem.2014.03.030
Fukui, K., Ito, S., Ueno, K., et al. (2011). New branching inhibitors and their potential as strigolactone mimics in rice. Bioorganic Med Chem Lett, 21, 4905–4908. https://doi.org/10.1016/j.bmcl.2011.06.019
Jia, K. P., Kountche, B. A., Jamil, M., et al. (2016). Nitro-phenlactone, a carlactone analog with pleiotropic strigolactone activities. Molecular Plant, 9, 1341–1344.
Jamil, M., Kountche, B. A., Haider, I., et al. (2018). Methyl phenlactonoates are efficient strigolactone analogs with simple structure. Journal of Experimental Botany, 69, 2319–2331. https://doi.org/10.1093/jxb/erx438
Janda, M., & Ruelland, E. (2015). Magical mystery tour: Salicylic acid signalling. Environmental and Experimental Botany, 114, 117–128. https://doi.org/10.1016/j.envexpbot.2014.07.003
Yang, L., Li, B., Zheng, X. Y., et al. (2015). Salicylic acid biosynthesis is enhanced and contributes to increased biotrophic pathogen resistance in Arabidopsis hybrids. Nature Communications. https://doi.org/10.1038/ncomms8309
Bernsdorff, F., Döring, A. C., Gruner, K., et al. (2016). Pipecolic acid orchestrates plant systemic acquired resistance and defense priming via salicylic acid-dependent and -independent pathways. The Plant Cell, 28, 102–129. https://doi.org/10.1105/tpc.15.00496
Lee, S., Kim, S. G., & Park, C. M. (2010). Salicylic acid promotes seed germination under high salinity by modulating antioxidant activity in Arabidopsis. New Phytologist, 188, 626–637. https://doi.org/10.1111/j.1469-8137.2010.03378.x
Prodhan, M. Y., Munemasa, S., Nahar, M. N. E. N., et al. (2018). Guard cell salicylic acid signaling is integrated into abscisic acid signaling via the Ca2+/CPK-dependent pathway. Plant Physiology, 178, 441–450. https://doi.org/10.1104/pp.18.00321
Šašek, V., Janda, M., Delage, E., et al. (2014). Constitutive salicylic acid accumulation in pi4kIIIβ1β2 Arabidopsis plants stunts rosette but not root growth. New Phytologist, 203, 805–816. https://doi.org/10.1111/nph.12822
Mou, Z., Fan, W., & Dong, X. (2003). Inducers of plant systemic acquired resistance Regulate NPR1 function through redox changes. Cell, 113, 935–944. https://doi.org/10.1016/S0092-8674(03)00429-X
Jin, H., Choi, S. M., Kang, M. J., et al. (2018). Salicylic acid-induced transcriptional reprogramming by the HAC-NPR1-TGA histone acetyltransferase complex in Arabidopsis. Nucleic Acids Research, 46, 11712–11725. https://doi.org/10.1093/nar/gky847
Wang, W., Withers, J., Li, H., et al. (2020). Structural basis of salicylic acid perception by Arabidopsis NPR proteins. Nature, 586, 311–316. https://doi.org/10.1038/s41586-020-2596-y
Rong, D., Luo, N., Mollet, J. C., et al. (2016). Salicylic Acid Regulates Pollen Tip Growth through an NPR3/NPR4-Independent Pathway. Molecular Plant, 9, 1478–1491. https://doi.org/10.1016/j.molp.2016.07.010
Chen, Z., Ricigliano, J. W., & Klessig, D. F. (1993). Purification and characterization of a soluble salicylic acid-binding protein from tobacco. Proceedings of the National Academy of Sciences of the United States of America, 90, 9533–9537. https://doi.org/10.1073/pnas.90.20.9533
Du, H., & Klessig, D. F. (1997). Identification of a soluble, high-affinity salicylic acid-binding protein in tobacco. Plant Physiology, 113, 1319–1327. https://doi.org/10.1104/pp.113.4.1319
Slaymaker, D. H., Navarre, D. A., Clark, D., et al. (2002). The tobacco salicylic acid-binding protein 3 (SABP3) is the chloroplast carbonic anhydrase, which exhibits antioxidant activity and plays a role in the hypersensitive defense response. Proceedings of the National Academy of Sciences of the United States of America, 99, 11640–11645. https://doi.org/10.1073/pnas.182427699
Tian, M., Caroline, C. V. D., Liu, P. P., et al. (2012). The combined use of photoaffinity labeling and surface plasmon resonance-based technology identifies multiple salicylic acid-binding proteins. The Plant Journal, 72, 1027–1038. https://doi.org/10.1111/tpj.12016
Manohar, M., Tian, M., Moreau, M., et al. (2015). Identification of multiple salicylic acid-binding proteins using two high throughput screens. Frontiers in Plant Science. https://doi.org/10.3389/fpls.2014.00777
Westfall CS, Zubieta C, Herrmann J, et al (2012) Structural basis for prereceptor modulation of plant hormones by gh3 proteins. Science (80- ) 336:1708–1711. https://doi.org/10.1126/science.1221863
Tian, M., Sasvari, Z., Gonzalez, P. A., et al. (2015). Salicylic acid inhibits the replication of Tomato bushy stunt virus by directly targeting a host component in the replication complex. Molecular Reproduction & Development, 28, 379–386. https://doi.org/10.1094/MPMI-09-14-0259-R
Liao, Y., Tian, M., Zhang, H., et al. (2015). Salicylic acid binding of mitochondrial alpha-ketoglutarate dehydrogenase E2 affects mitochondrial oxidative phosphorylation and electron transport chain components and plays a role in basal defense against tobacco mosaic virus in tomato. New Phytologist, 205, 1296–1307. https://doi.org/10.1111/nph.13137
Moreau, M., Westlake, T., Zampogna, G., et al. (2013). The Arabidopsis oligopeptidases TOP1 and TOP2 are salicylic acid targets that modulate SA-mediated signaling and the immune response. The Plant Journal, 76, 603–614. https://doi.org/10.1111/tpj.12320
Manohar, M., Choi, H. W., Manosalva, P., et al. (2017). Plant and human MORC proteins have DNA-modifying activities similar to type II topoisomerases, but require one or more additional factors for full activity. Molecular Reproduction & Development, 30, 87–100. https://doi.org/10.1094/MPMI-10-16-0208-R
Choi, H. W., Manohar, M., Manosalva, P., et al. (2016). Activation of plant innate immunity by extracellular high mobility group Box 3 and its inhibition by salicylic acid. PLoS Pathogens. https://doi.org/10.1371/journal.ppat.1005518
Round, A., Brown, E., Marcellin, R., et al. (2013). Determination of the GH3.12 protein conformation through HPLC-integrated SAXS measurements combined with X-ray crystallography. Acta Crystallographica, Section D: Biological Crystallography, 69, 2072–2080. https://doi.org/10.1107/S0907444913019276
Zambounis, A. G., Kalamaki, M. S., Tani, E. E., et al. (2012). Expression analysis of defense-related genes in cotton (Gossypium hirsutum) after Fusarium oxysporum f. sp. vasinfectum infection and following chemical elicitation using a salicylic acid analog and methyl jasmonate. Plant Molecular Biology Reporter, 30, 225–234. https://doi.org/10.1007/s11105-011-0335-0
Faize, L., & Faize, M. (2018). Functional analogues of salicylic acid and their use in crop protection. Agronomy, 8(1), 5.
Acknowledgements
Authors are thankful to Department of Microbiology and Biotechnology, School of Sciences, Gujarat University, DST-FIST Sponsored Department, for providing necessary facilities to perform experiments. We acknowledge Education Department, Government of Gujarat, India for the providing research fellowship to Rohit Patel and Krina Mehta under the ScHeme Of Developing High-quality research (SHODH).
Funding
Authors are also thankful to UGC (Start-up Research Grant) for providing fund under the F.30–521/2020(BSR), Under Secretary FD-III Section, University Grant Commission, New Delhi 110002.
Author information
Authors and Affiliations
Contributions
RP and KM wrote the first draft. DG and MS finalized the manuscript.
Corresponding authors
Ethics declarations
Conflict of interest
On behalf of all authors, the corresponding author states that there is no conflict of interest.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Patel, R., Mehta, K., Goswami, D. et al. An Anecdote on Prospective Protein Targets for Developing Novel Plant Growth Regulators. Mol Biotechnol 64, 109–129 (2022). https://doi.org/10.1007/s12033-021-00404-w
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s12033-021-00404-w