Pub Date : 2026-01-05DOI: 10.1038/s41477-025-02185-5
Meng Peng, Jin Li, Xinyu Liu, Anran Liu, Barbara De Meester, Marlies Brouckaert, Geert Goeminne, Kris Morreel, Yanding Li, Vitaliy I. Timokhin, Ruben Vanholme, John Ralph, Wout Boerjan
Chorismate is a branch-point metabolite in the biosynthesis of aromatic amino acids, vitamins, antibiotics and various other aromatic products in bacteria, fungi and plants. Although 13 chorismate-utilizing enzymes have been identified in bacteria, only 6 have been described in plants, where an estimated 30% of all photosynthetically fixed carbon passes through chorismate. Here we describe a biosynthetic gene cluster (BGC) consisting of five core genes, including two reductases, two methyltransferases and one glucosyltransferase. Genetic and biochemical evidence shows that these five enzymes collectively give rise to three biosynthetic pathways, each originating from chorismate: two parallel pathways produce a class of non-aromatic, isomeric compounds abundant in the roots of Arabidopsis thaliana, whereas the third pathway produces methylated and glucosylated chorismate derivatives that subsequently react non-enzymatically with glutathione. Genome analysis revealed that variants of this BGC are present in some but not all species in the Brassicaceae family. Taken together, our study uncovered a BGC, containing three chorismate-utilizing enzymes, that controls three distinct post-chorismate pathways in A. thaliana. This work not only advances our understanding of carbon flow in this model plant but also highlights that the biochemical complexity encoded by plant BGCs is greater than previously appreciated. Peng et al. identify a class of non-aromatic, chorismate-derived compounds, abundant in the roots of Arabidopsis thaliana. These compounds are made by a biosynthetic gene cluster comprising five adjacent genes encoding biosynthetic enzymes.
{"title":"A biosynthetic gene cluster for three post-chorismate pathways in Arabidopsis","authors":"Meng Peng, Jin Li, Xinyu Liu, Anran Liu, Barbara De Meester, Marlies Brouckaert, Geert Goeminne, Kris Morreel, Yanding Li, Vitaliy I. Timokhin, Ruben Vanholme, John Ralph, Wout Boerjan","doi":"10.1038/s41477-025-02185-5","DOIUrl":"10.1038/s41477-025-02185-5","url":null,"abstract":"Chorismate is a branch-point metabolite in the biosynthesis of aromatic amino acids, vitamins, antibiotics and various other aromatic products in bacteria, fungi and plants. Although 13 chorismate-utilizing enzymes have been identified in bacteria, only 6 have been described in plants, where an estimated 30% of all photosynthetically fixed carbon passes through chorismate. Here we describe a biosynthetic gene cluster (BGC) consisting of five core genes, including two reductases, two methyltransferases and one glucosyltransferase. Genetic and biochemical evidence shows that these five enzymes collectively give rise to three biosynthetic pathways, each originating from chorismate: two parallel pathways produce a class of non-aromatic, isomeric compounds abundant in the roots of Arabidopsis thaliana, whereas the third pathway produces methylated and glucosylated chorismate derivatives that subsequently react non-enzymatically with glutathione. Genome analysis revealed that variants of this BGC are present in some but not all species in the Brassicaceae family. Taken together, our study uncovered a BGC, containing three chorismate-utilizing enzymes, that controls three distinct post-chorismate pathways in A. thaliana. This work not only advances our understanding of carbon flow in this model plant but also highlights that the biochemical complexity encoded by plant BGCs is greater than previously appreciated. Peng et al. identify a class of non-aromatic, chorismate-derived compounds, abundant in the roots of Arabidopsis thaliana. These compounds are made by a biosynthetic gene cluster comprising five adjacent genes encoding biosynthetic enzymes.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"12 1","pages":"205-216"},"PeriodicalIF":13.6,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145902662","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-05DOI: 10.1038/s41477-025-02179-3
Zhijie Ren, Zebin Liu, Yasheng Xi, Yuxin Dong, Lei Gao, Qifei Gao, Congcong Hou, Sheng Luan, Legong Li, Wang Tian
Calcium (Ca2+) is an essential macronutrient for plant growth and defence, yet the molecular mechanisms regulating its uptake from soil remain largely undefined. Through bioinformatics and electrophysiological screening, we identified a group of plant-specific proteins, named the IONIC CURRENT FAMILY A (ICAs), which confer Ca2+-permeable non-selective cation channel (CNCC) activities in heterologous systems. In Arabidopsis thaliana, AtICA1, AtICA2, AtICA3 and AtICA4 are predominantly expressed in root cells, and their proteins localize to the plasma membrane. Under either limited or excessive external Ca2+ conditions, ica1/2/3/4 quadruple mutants display hypersensitivity or reduced sensitivity, respectively, as evidenced by altered root length. In addition, these mutants show increased sensitivity to various abiotic and biotic stresses under normal Ca2+ conditions. The ica mutants lack the previously characterized CNCC-mediated currents in roots that facilitate cellular Ca2+ uptake, resulting in lower Ca2+ levels compared with wild-type (WT) plants. Our findings suggest that AtICA1/2/3/4 may function as components of CNCCs, mediating Ca2+ uptake crucial for broad environmental stress tolerance under normal Ca2+ conditions. This study provides molecular insight into the mechanisms governing Ca2+ uptake in plant roots and expands our understanding of how plants maintain Ca2+ homeostasis under varying environmental conditions. This study identifies ICA proteins in Arabidopsis roots as key mediators of Ca2+ uptake through non-selective cation channels. High-order ica mutants show reduced Ca2+ levels and heightened stress sensitivity, revealing ICAs’ role in Ca2+ homeostasis.
{"title":"Arabidopsis IONIC CURRENT FAMILY A proteins facilitate environmental calcium acquisition essential for stress tolerance","authors":"Zhijie Ren, Zebin Liu, Yasheng Xi, Yuxin Dong, Lei Gao, Qifei Gao, Congcong Hou, Sheng Luan, Legong Li, Wang Tian","doi":"10.1038/s41477-025-02179-3","DOIUrl":"10.1038/s41477-025-02179-3","url":null,"abstract":"Calcium (Ca2+) is an essential macronutrient for plant growth and defence, yet the molecular mechanisms regulating its uptake from soil remain largely undefined. Through bioinformatics and electrophysiological screening, we identified a group of plant-specific proteins, named the IONIC CURRENT FAMILY A (ICAs), which confer Ca2+-permeable non-selective cation channel (CNCC) activities in heterologous systems. In Arabidopsis thaliana, AtICA1, AtICA2, AtICA3 and AtICA4 are predominantly expressed in root cells, and their proteins localize to the plasma membrane. Under either limited or excessive external Ca2+ conditions, ica1/2/3/4 quadruple mutants display hypersensitivity or reduced sensitivity, respectively, as evidenced by altered root length. In addition, these mutants show increased sensitivity to various abiotic and biotic stresses under normal Ca2+ conditions. The ica mutants lack the previously characterized CNCC-mediated currents in roots that facilitate cellular Ca2+ uptake, resulting in lower Ca2+ levels compared with wild-type (WT) plants. Our findings suggest that AtICA1/2/3/4 may function as components of CNCCs, mediating Ca2+ uptake crucial for broad environmental stress tolerance under normal Ca2+ conditions. This study provides molecular insight into the mechanisms governing Ca2+ uptake in plant roots and expands our understanding of how plants maintain Ca2+ homeostasis under varying environmental conditions. This study identifies ICA proteins in Arabidopsis roots as key mediators of Ca2+ uptake through non-selective cation channels. High-order ica mutants show reduced Ca2+ levels and heightened stress sensitivity, revealing ICAs’ role in Ca2+ homeostasis.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"12 1","pages":"125-139"},"PeriodicalIF":13.6,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145902656","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-05DOI: 10.1038/s41477-025-02184-6
Han Xiao, Xing-Xing Shi, Min Li, You-Wang Wang, Da-Wei Wang, Long-Can Mei, Hong-Yan Lin, Ping Zhu, Guang-Fu Yang
Solanesyl diphosphate synthase (SPS) is crucial for photosynthesis, as it supplies prenyl precursors for the biosynthesis of the photosynthetic electron carrier, plastoquinone-9 (PQ-9). Fibrillin 5 (FBN5) stimulates SPS catalytic activity through direct binding, which is essential for normal plant growth. However, the molecular mechanism of FBN5-mediated SPS catalytic regulation remains unclear. In Oryza sativa (rice), OsSPS3 is an important plastid-localized SPS isoform involved in PQ-9 formation. The Osfbn5 mutant plants display photodamage with exacerbated PQ-9 deficiency when exposed to high light. Here rice serves as a model organism to study SPS and FBN5. We report the crystal structures of the apo and inhibitor-bound forms of OsSPS3, revealing the alternating catalytic mechanism of the asymmetric OsSPS3 dimer. In addition, we report the cryo-electron microscopy structures of the apo and ligand-bound forms of the OsSPS3–FBN5 complex, showing that OsFBN5 binding triggers an open-to-closed conformational transition of a lid-like capping loop within the inactive monomer of OsSPS3, allowing both monomers of dimeric OsSPS3 to be catalytically active. A comparison of the enzymatic activities of the wild-type OsSPS3 homodimer and a recombinant OsSPS3 heterodimer containing one inactive mutant subunit revealed that OsFBN5 enhances the activity of OsSPS3 by inducing a synchronous catalytic mechanism. This work reveals the dynamic catalytic mechanism of OsSPS3 and provides a structural basis for understanding its function and the FBN5-mediated regulation of the PQ-9 biosynthesis pathway. This study provides structural insight into the dynamic catalytic mechanism of OsSPS3, a key enzyme in plastoquinone-9 biosynthesis. OsFBN5 enhances the activity of the OsSPS3 dimer by shifting its catalytic mechanism from alternating to synchronous.
{"title":"Structural insights into the molecular mechanisms of OsFBN5-induced OsSPS3 catalysis","authors":"Han Xiao, Xing-Xing Shi, Min Li, You-Wang Wang, Da-Wei Wang, Long-Can Mei, Hong-Yan Lin, Ping Zhu, Guang-Fu Yang","doi":"10.1038/s41477-025-02184-6","DOIUrl":"10.1038/s41477-025-02184-6","url":null,"abstract":"Solanesyl diphosphate synthase (SPS) is crucial for photosynthesis, as it supplies prenyl precursors for the biosynthesis of the photosynthetic electron carrier, plastoquinone-9 (PQ-9). Fibrillin 5 (FBN5) stimulates SPS catalytic activity through direct binding, which is essential for normal plant growth. However, the molecular mechanism of FBN5-mediated SPS catalytic regulation remains unclear. In Oryza sativa (rice), OsSPS3 is an important plastid-localized SPS isoform involved in PQ-9 formation. The Osfbn5 mutant plants display photodamage with exacerbated PQ-9 deficiency when exposed to high light. Here rice serves as a model organism to study SPS and FBN5. We report the crystal structures of the apo and inhibitor-bound forms of OsSPS3, revealing the alternating catalytic mechanism of the asymmetric OsSPS3 dimer. In addition, we report the cryo-electron microscopy structures of the apo and ligand-bound forms of the OsSPS3–FBN5 complex, showing that OsFBN5 binding triggers an open-to-closed conformational transition of a lid-like capping loop within the inactive monomer of OsSPS3, allowing both monomers of dimeric OsSPS3 to be catalytically active. A comparison of the enzymatic activities of the wild-type OsSPS3 homodimer and a recombinant OsSPS3 heterodimer containing one inactive mutant subunit revealed that OsFBN5 enhances the activity of OsSPS3 by inducing a synchronous catalytic mechanism. This work reveals the dynamic catalytic mechanism of OsSPS3 and provides a structural basis for understanding its function and the FBN5-mediated regulation of the PQ-9 biosynthesis pathway. This study provides structural insight into the dynamic catalytic mechanism of OsSPS3, a key enzyme in plastoquinone-9 biosynthesis. OsFBN5 enhances the activity of the OsSPS3 dimer by shifting its catalytic mechanism from alternating to synchronous.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"12 1","pages":"217-230"},"PeriodicalIF":13.6,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145903375","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-02DOI: 10.1038/s41477-025-02161-z
Chloé Cathebras, Xiaoyun Gong, Rosa Elena Andrade, Ksenia Vondenhoff, Jean Keller, Pierre-Marc Delaux, Makoto Hayashi, Maximilian Griesmann, Martin Parniske
The root nodule symbiosis of plants with nitrogen-fixing bacteria is phylogenetically restricted to a single clade of flowering plants, which calls for as yet unidentified trait acquisitions and genetic changes in the last common ancestor. Here we discovered—within the promoter of the transcription factor gene Nodule Inception (NIN)—a cis-regulatory element (PACE), exclusively present in members of this clade. PACE was essential for restoring infection threads in nin mutants of the legume Lotus japonicus. PACE sequence variants from root nodule symbiosis-competent species appeared functionally equivalent. Evolutionary loss or mutation of PACE is associated with loss of this symbiosis. During the early stages of nodule development, PACE dictates gene expression in a spatially restricted domain containing cortical cells carrying infection threads. Consistent with its expression domain, PACE-driven NIN expression restored the formation of cortical infection threads, also when engineered into the NIN promoter of tomato. Our data pinpoint PACE as a key evolutionary invention that connected NIN to a pre-existing symbiosis signal transduction cascade that governs the intracellular accommodation of arbuscular mycorrhiza fungi and is conserved throughout land plants. This connection enabled bacterial uptake into plant cells via intracellular support structures such as infection threads, a unique and unifying feature of this symbiosis. A key step in the evolution of the nitrogen-fixing root nodule symbiosis, occurring 100 million years ago, subjected the control of Nodule Inception (NIN) gene expression to a protein complex that regulated transcription much earlier in the arbuscular mycorrhiza symbiosis.
{"title":"A novel cis-element enabled bacterial uptake by plant cells","authors":"Chloé Cathebras, Xiaoyun Gong, Rosa Elena Andrade, Ksenia Vondenhoff, Jean Keller, Pierre-Marc Delaux, Makoto Hayashi, Maximilian Griesmann, Martin Parniske","doi":"10.1038/s41477-025-02161-z","DOIUrl":"10.1038/s41477-025-02161-z","url":null,"abstract":"The root nodule symbiosis of plants with nitrogen-fixing bacteria is phylogenetically restricted to a single clade of flowering plants, which calls for as yet unidentified trait acquisitions and genetic changes in the last common ancestor. Here we discovered—within the promoter of the transcription factor gene Nodule Inception (NIN)—a cis-regulatory element (PACE), exclusively present in members of this clade. PACE was essential for restoring infection threads in nin mutants of the legume Lotus japonicus. PACE sequence variants from root nodule symbiosis-competent species appeared functionally equivalent. Evolutionary loss or mutation of PACE is associated with loss of this symbiosis. During the early stages of nodule development, PACE dictates gene expression in a spatially restricted domain containing cortical cells carrying infection threads. Consistent with its expression domain, PACE-driven NIN expression restored the formation of cortical infection threads, also when engineered into the NIN promoter of tomato. Our data pinpoint PACE as a key evolutionary invention that connected NIN to a pre-existing symbiosis signal transduction cascade that governs the intracellular accommodation of arbuscular mycorrhiza fungi and is conserved throughout land plants. This connection enabled bacterial uptake into plant cells via intracellular support structures such as infection threads, a unique and unifying feature of this symbiosis. A key step in the evolution of the nitrogen-fixing root nodule symbiosis, occurring 100 million years ago, subjected the control of Nodule Inception (NIN) gene expression to a protein complex that regulated transcription much earlier in the arbuscular mycorrhiza symbiosis.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"12 1","pages":"140-151"},"PeriodicalIF":13.6,"publicationDate":"2026-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41477-025-02161-z.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145892624","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Rice roots develop aerenchyma, which transports oxygen from shoots to roots, facilitating adaptation to waterlogged conditions. This oxygen oxidizes ferrous ions into ferric compounds, forming iron plaque that mitigates iron toxicity. However, the molecular mechanisms linking aerenchyma and iron plaque formation remain poorly understood. Here we identified a rice mutant (AZ1302) defective in both aerenchyma and iron plaque formation, with the causal mutation mapped to the PHYTOENE SYNTHASE 2 (OsPSY2) gene. CRISPR–Cas9-induced psy2 mutants exhibited reduced levels of carotenoid-derived hormones, strigolactones and abscisic acid, in roots. In psy2 mutants, exogenous application of strigolactones rescued aerenchyma formation, while abscisic acid restored iron plaque deposition, providing evidence for distinct hormonal regulatory functions in the two processes. These findings revise the current understanding by dissociating the roles of aerenchyma and iron plaque formation, establishing a role for OsPSY2 in integrating hormonal signalling to drive root plasticity and offering new insights into plant adaptation under environmental stress. Shrestha et al. reveal that rice PHYTOENE SYNTHASE 2 (OsPSY2) coordinates the carotenoid-derived biosynthesis of abscisic acid and strigolactones, which independently govern iron plaque deposition and aerenchyma development, respectively.
{"title":"Carotenoid biosynthesis drives root plasticity through aerenchyma and iron plaque formation in rice","authors":"Jeevan Kumar Shrestha, Chih-Yu Lin, Jian You Wang, I-Chien Tang, Chun-Hao Hu, Munkhtsetseg Tsednee, Yasha Zhang, Muhammad Jamil, Lamis Berqdar, Ikram Blilou, Salim Al-Babili, Chang-Sheng Wang, Kuo-Chen Yeh","doi":"10.1038/s41477-025-02170-y","DOIUrl":"10.1038/s41477-025-02170-y","url":null,"abstract":"Rice roots develop aerenchyma, which transports oxygen from shoots to roots, facilitating adaptation to waterlogged conditions. This oxygen oxidizes ferrous ions into ferric compounds, forming iron plaque that mitigates iron toxicity. However, the molecular mechanisms linking aerenchyma and iron plaque formation remain poorly understood. Here we identified a rice mutant (AZ1302) defective in both aerenchyma and iron plaque formation, with the causal mutation mapped to the PHYTOENE SYNTHASE 2 (OsPSY2) gene. CRISPR–Cas9-induced psy2 mutants exhibited reduced levels of carotenoid-derived hormones, strigolactones and abscisic acid, in roots. In psy2 mutants, exogenous application of strigolactones rescued aerenchyma formation, while abscisic acid restored iron plaque deposition, providing evidence for distinct hormonal regulatory functions in the two processes. These findings revise the current understanding by dissociating the roles of aerenchyma and iron plaque formation, establishing a role for OsPSY2 in integrating hormonal signalling to drive root plasticity and offering new insights into plant adaptation under environmental stress. Shrestha et al. reveal that rice PHYTOENE SYNTHASE 2 (OsPSY2) coordinates the carotenoid-derived biosynthesis of abscisic acid and strigolactones, which independently govern iron plaque deposition and aerenchyma development, respectively.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"12 1","pages":"179-190"},"PeriodicalIF":13.6,"publicationDate":"2026-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41477-025-02170-y.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145892682","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-17DOI: 10.1038/s41477-025-02159-7
W. Zierer, M. Fritzler, T. J. Chiu, R. B. Anjanappa, S.-H. Chang, R. Metzner, J. Quiros, C. E. Lamm, M. Thieme, R. Koller, G. Huber, O. Muller, U. Rascher, U. Sonnewald, H. E. Neuhaus, W. Gruissem, L. Bellin
Cassava (Manihot esculenta) is an important crop for food security in the tropics, particularly for smallholder farmers in sub-Saharan Africa, where yields are often severely limited by pathogen pressure, nutrient deficiency and water scarcity. We expressed a non-rectifying Arabidopsis thaliana potassium (K+) channel gene version, AKT2var, in the vascular tissue of cassava plants. The transgenic cassava plants had higher electron transport and CO2 assimilation rates, a higher bulk flow velocity and increased source–sink carbohydrate transport, as demonstrated by comparative 11C-positron emission tomography and tissue-specific metabolite profiling. Cassava storage root yield was significantly increased in greenhouse experiments and in a multi-year field trial conducted under subtropical conditions. AKT2var plants were also more tolerant of drought stress and had higher storage root yield. Targeted alteration of K+ transport is therefore a promising strategy to improve cassava productivity without additional fertilizer input and in climate-adverse growing conditions. Zierer et al. engineered cassava to express a modified potassium channel that enhances sugar flow, improving the yield and drought resilience. This strategy offers a route to increase cassava productivity in tropical regions.
{"title":"Engineering vascular potassium transport increases yield and drought resilience of cassava","authors":"W. Zierer, M. Fritzler, T. J. Chiu, R. B. Anjanappa, S.-H. Chang, R. Metzner, J. Quiros, C. E. Lamm, M. Thieme, R. Koller, G. Huber, O. Muller, U. Rascher, U. Sonnewald, H. E. Neuhaus, W. Gruissem, L. Bellin","doi":"10.1038/s41477-025-02159-7","DOIUrl":"10.1038/s41477-025-02159-7","url":null,"abstract":"Cassava (Manihot esculenta) is an important crop for food security in the tropics, particularly for smallholder farmers in sub-Saharan Africa, where yields are often severely limited by pathogen pressure, nutrient deficiency and water scarcity. We expressed a non-rectifying Arabidopsis thaliana potassium (K+) channel gene version, AKT2var, in the vascular tissue of cassava plants. The transgenic cassava plants had higher electron transport and CO2 assimilation rates, a higher bulk flow velocity and increased source–sink carbohydrate transport, as demonstrated by comparative 11C-positron emission tomography and tissue-specific metabolite profiling. Cassava storage root yield was significantly increased in greenhouse experiments and in a multi-year field trial conducted under subtropical conditions. AKT2var plants were also more tolerant of drought stress and had higher storage root yield. Targeted alteration of K+ transport is therefore a promising strategy to improve cassava productivity without additional fertilizer input and in climate-adverse growing conditions. Zierer et al. engineered cassava to express a modified potassium channel that enhances sugar flow, improving the yield and drought resilience. This strategy offers a route to increase cassava productivity in tropical regions.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 12","pages":"2498-2510"},"PeriodicalIF":13.6,"publicationDate":"2025-12-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41477-025-02159-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145765582","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-17DOI: 10.1038/s41477-025-02167-7
Leena Tripathi
Engineering cassava with a modified potassium (K+) channel gene from Arabidopsis thaliana enhances K+ transport, photosynthesis and storage root yield, offering a sustainable strategy to boost productivity and resilience in nutrient-poor and drought-prone environments.
{"title":"Engineering cassava for smart potassium use","authors":"Leena Tripathi","doi":"10.1038/s41477-025-02167-7","DOIUrl":"10.1038/s41477-025-02167-7","url":null,"abstract":"Engineering cassava with a modified potassium (K+) channel gene from Arabidopsis thaliana enhances K+ transport, photosynthesis and storage root yield, offering a sustainable strategy to boost productivity and resilience in nutrient-poor and drought-prone environments.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 12","pages":"2451-2452"},"PeriodicalIF":13.6,"publicationDate":"2025-12-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145766421","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-17DOI: 10.1038/s41477-025-02203-6
December is a time when ‘… of the Year’ pieces appear in all kinds of publications. For this year only, Nature Plants is joining the trend.
12月是“年度……”出现在各种出版物上的时候。今年，自然植物也加入了这一潮流。
{"title":"… of the Year","authors":"","doi":"10.1038/s41477-025-02203-6","DOIUrl":"10.1038/s41477-025-02203-6","url":null,"abstract":"December is a time when ‘… of the Year’ pieces appear in all kinds of publications. For this year only, Nature Plants is joining the trend.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 12","pages":"2439-2439"},"PeriodicalIF":13.6,"publicationDate":"2025-12-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41477-025-02203-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145766422","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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