Pub Date : 2024-10-04DOI: 10.1038/s41477-024-01814-9
Philippe Johann to Berens, Jackson Peter, Sandrine Koechler, Mathieu Bruggeman, Sébastien Staerck, Jean Molinier
Plants have evolved sophisticated DNA repair mechanisms to cope with the deleterious effects of ultraviolet (UV)-induced DNA damage. Indeed, DNA repair pathways cooperate with epigenetic-related processes to efficiently maintain genome integrity. However, it remains to be deciphered how photodamages are recognized within different chromatin landscapes, especially in compacted genomic regions such as constitutive heterochromatin. Here we combined cytogenetics and epigenomics to identify that UV-C irradiation induces modulation of the main epigenetic mark found in constitutive heterochromatin, H3K9me2. We demonstrated that the histone demethylase, Jumonji27 (JMJ27), contributes to the UV-induced reduction of H3K9me2 content at chromocentres. In addition, we identified that JMJ27 forms a complex with the photodamage recognition factor, DNA Damage Binding protein 2 (DDB2), and that the fine-tuning of H3K9me2 contents orchestrates DDB2 dynamics on chromatin in response to UV-C exposure. Hence, this study uncovers the unexpected existence of an interplay between photodamage repair and H3K9me2 homeostasis. UV exposure modulates H3K9me2 contents at chromocentres via the histone demethylase JMJ27 which interacts with the DNA damage recognition factor, DDB2, and facilitates photodamage repair. The loading or release of DDB2 at nucleosome sites is optimized by the fine-tuning of H3K9me2.
植物进化出了复杂的 DNA 修复机制，以应对紫外线（UV）引起的 DNA 损伤的有害影响。事实上，DNA 修复途径与表观遗传相关过程合作，有效地维护了基因组的完整性。然而，光损伤是如何在不同的染色质景观中被识别的，尤其是在紧密的基因组区域，如组成型异染色质中，仍有待破译。在这里，我们将细胞遗传学和表观基因组学结合起来，发现紫外线-C 照射会诱导改变构成型异染色质中的主要表观遗传标记 H3K9me2。我们证明，组蛋白去甲基化酶 Jumonji27（JMJ27）有助于紫外线诱导的染色体中心 H3K9me2 含量的减少。此外，我们还发现 JMJ27 与光损伤识别因子 DNA 损伤结合蛋白 2（DDB2）形成复合物，而 H3K9me2 含量的微调是 DDB2 在染色质上响应紫外线-C 暴露的动态协调。因此，这项研究发现了光损伤修复与 H3K9me2 平衡之间意想不到的相互作用。
{"title":"The histone demethylase JMJ27 acts during the UV-induced modulation of H3K9me2 landscape and facilitates photodamage repair","authors":"Philippe Johann to Berens, Jackson Peter, Sandrine Koechler, Mathieu Bruggeman, Sébastien Staerck, Jean Molinier","doi":"10.1038/s41477-024-01814-9","DOIUrl":"10.1038/s41477-024-01814-9","url":null,"abstract":"Plants have evolved sophisticated DNA repair mechanisms to cope with the deleterious effects of ultraviolet (UV)-induced DNA damage. Indeed, DNA repair pathways cooperate with epigenetic-related processes to efficiently maintain genome integrity. However, it remains to be deciphered how photodamages are recognized within different chromatin landscapes, especially in compacted genomic regions such as constitutive heterochromatin. Here we combined cytogenetics and epigenomics to identify that UV-C irradiation induces modulation of the main epigenetic mark found in constitutive heterochromatin, H3K9me2. We demonstrated that the histone demethylase, Jumonji27 (JMJ27), contributes to the UV-induced reduction of H3K9me2 content at chromocentres. In addition, we identified that JMJ27 forms a complex with the photodamage recognition factor, DNA Damage Binding protein 2 (DDB2), and that the fine-tuning of H3K9me2 contents orchestrates DDB2 dynamics on chromatin in response to UV-C exposure. Hence, this study uncovers the unexpected existence of an interplay between photodamage repair and H3K9me2 homeostasis. UV exposure modulates H3K9me2 contents at chromocentres via the histone demethylase JMJ27 which interacts with the DNA damage recognition factor, DDB2, and facilitates photodamage repair. The loading or release of DDB2 at nucleosome sites is optimized by the fine-tuning of H3K9me2.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 11","pages":"1698-1709"},"PeriodicalIF":15.8,"publicationDate":"2024-10-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142374252","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 : 2024-10-04DOI: 10.1038/s41477-024-01821-w
Pengcheng Hu, Yanmei Xu, Yanhua Su, Yuxin Wang, Yan Xiong, Yong Ding
Phosphorylation of histone H3 at threonine 11 (H3T11ph) affects transcription and chromosome stability. However, the enzymes responsible for depositing H3T11ph and the functions of H3T11ph in plants remain unknown. Here we report that in Arabidopsis thaliana, PYRUVATE KINASE 6 (PK6), PK7 and PK8 enter the nucleus under conditions of sufficient glucose and light exposure, where they interact with SWI2/SNF2-RELATED 1 COMPLEX 4 (SWC4) and phosphorylate H3 at threonine 11. Mutations in these kinases or knockdown of SWC4 resulted in FLC-dependent early flowering, short hypocotyls and short pedicels. Genome-wide, H3T11ph is highly enriched at transcription start sites and transcription termination sites, and positively correlated with gene transcript levels. PK6 and SWC4 targeted FLC, MYB73, PRE1, TCP4 and TCP10, depositing H3T11ph at these loci and promoting their transcription, and PK6 occupancy at these loci requires SWC4. Together, our results reveal that nuclear-localized PK6, PK7 and PK8 modulate H3T11ph and plant growth. This study reports that the nucleocytoplasmic shuttling of pyruvate kinase 6 (PK6), PK7 and PK8 mediates phosphorylation of H3 at threonine 11, represses flowering time, and promotes hypocotyl and pedicel elongation in Arabidopsis.
{"title":"Nuclear-localized pyruvate kinases control phosphorylation of histone H3 on threonine 11","authors":"Pengcheng Hu, Yanmei Xu, Yanhua Su, Yuxin Wang, Yan Xiong, Yong Ding","doi":"10.1038/s41477-024-01821-w","DOIUrl":"10.1038/s41477-024-01821-w","url":null,"abstract":"Phosphorylation of histone H3 at threonine 11 (H3T11ph) affects transcription and chromosome stability. However, the enzymes responsible for depositing H3T11ph and the functions of H3T11ph in plants remain unknown. Here we report that in Arabidopsis thaliana, PYRUVATE KINASE 6 (PK6), PK7 and PK8 enter the nucleus under conditions of sufficient glucose and light exposure, where they interact with SWI2/SNF2-RELATED 1 COMPLEX 4 (SWC4) and phosphorylate H3 at threonine 11. Mutations in these kinases or knockdown of SWC4 resulted in FLC-dependent early flowering, short hypocotyls and short pedicels. Genome-wide, H3T11ph is highly enriched at transcription start sites and transcription termination sites, and positively correlated with gene transcript levels. PK6 and SWC4 targeted FLC, MYB73, PRE1, TCP4 and TCP10, depositing H3T11ph at these loci and promoting their transcription, and PK6 occupancy at these loci requires SWC4. Together, our results reveal that nuclear-localized PK6, PK7 and PK8 modulate H3T11ph and plant growth. This study reports that the nucleocytoplasmic shuttling of pyruvate kinase 6 (PK6), PK7 and PK8 mediates phosphorylation of H3 at threonine 11, represses flowering time, and promotes hypocotyl and pedicel elongation in Arabidopsis.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 11","pages":"1682-1697"},"PeriodicalIF":15.8,"publicationDate":"2024-10-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142374124","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}
Plant pathogens secrete numerous effectors to promote host infection, but whether any of these toxic proteins undergoes phase separation to manipulate plant defence and how the host copes with this event remain elusive. Here we show that the effector FolSvp2, which is secreted from the fungal pathogen Fusarium oxysporum f. sp. lycopersici (Fol), translocates a tomato iron-sulfur protein (SlISP) from plastids into effector condensates in planta via phase separation. Relocation of SlISP attenuates plant reactive oxygen species production and thus facilitates Fol invasion. The action of FolSvp2 also requires K205 acetylation that prevents ubiquitination-dependent degradation of this protein in both Fol and plant cells. However, tomato has evolved a defence protein, SlPR1. Apoplastic SlPR1 physically interacts with and inhibits FolSvp2 entry into host cells and, consequently, abolishes its deleterious effect. These findings reveal a previously unknown function of PR1 in countering a new mode of effector action. There is a continuous arms race between pathogens and their host plants. Li et al. reveal that PR1 prevents entry of a fungal effector into plant cells from the apoplast that otherwise would quench host defence oxidizing agents via phase separation.
{"title":"Plant PR1 rescues condensation of the plastid iron-sulfur protein by a fungal effector","authors":"Jingtao Li, Limei Yang, Shuzhi Ding, Mingming Gao, Yu Yan, Gang Yu, Yaning Zheng, Wenxing Liang","doi":"10.1038/s41477-024-01811-y","DOIUrl":"10.1038/s41477-024-01811-y","url":null,"abstract":"Plant pathogens secrete numerous effectors to promote host infection, but whether any of these toxic proteins undergoes phase separation to manipulate plant defence and how the host copes with this event remain elusive. Here we show that the effector FolSvp2, which is secreted from the fungal pathogen Fusarium oxysporum f. sp. lycopersici (Fol), translocates a tomato iron-sulfur protein (SlISP) from plastids into effector condensates in planta via phase separation. Relocation of SlISP attenuates plant reactive oxygen species production and thus facilitates Fol invasion. The action of FolSvp2 also requires K205 acetylation that prevents ubiquitination-dependent degradation of this protein in both Fol and plant cells. However, tomato has evolved a defence protein, SlPR1. Apoplastic SlPR1 physically interacts with and inhibits FolSvp2 entry into host cells and, consequently, abolishes its deleterious effect. These findings reveal a previously unknown function of PR1 in countering a new mode of effector action. There is a continuous arms race between pathogens and their host plants. Li et al. reveal that PR1 prevents entry of a fungal effector into plant cells from the apoplast that otherwise would quench host defence oxidizing agents via phase separation.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 11","pages":"1775-1789"},"PeriodicalIF":15.8,"publicationDate":"2024-10-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142374123","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 : 2024-10-04DOI: 10.1038/s41477-024-01791-z
Sonia E. Evans, Yuan Xu, Matthew E. Bergman, Scott A. Ford, Yingxia Liu, Thomas D. Sharkey, Michael A. Phillips
RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (Rubisco) produces pyruvate in the chloroplast through β-elimination of the aci-carbanion intermediate1. Here we show that this side reaction supplies pyruvate for isoprenoid, fatty acid and branched-chain amino acid biosynthesis in photosynthetically active tissue. 13C labelling studies of intact Arabidopsis plants demonstrate that the total carbon commitment to pyruvate is too large for phosphoenolpyruvate to serve as a precursor. Low oxygen stimulates Rubisco carboxylase activity and increases pyruvate production and flux through the 2-C-methyl-d-erythritol-4-phosphate (MEP) pathway, which supplies the precursors for plastidic isoprenoid biosynthesis2,3. Metabolome analysis of mutants defective in phosphoenolpyruvate or pyruvate import and biochemical characterization of isolated chloroplasts further support Rubisco as the main source of pyruvate in chloroplasts. Seedlings incorporated exogenous,13C-labelled pyruvate into MEP pathway intermediates, while adult plants did not, underscoring the developmental transition in pyruvate sourcing. Rubisco β-elimination leading to pyruvate constituted 0.7% of the product profile in in vitro assays, which translates to 2% of the total carbon leaving the Calvin–Benson–Bassham cycle. These insights solve the “pyruvate paradox”4, improve the fit of metabolic models for central metabolism and connect the MEP pathway directly to carbon assimilation. As nature’s most important enzyme, Rubisco fixes carbon dioxide in the Calvin–Benson–Bassham cycle. Its lesser-known side job is supplying pyruvate in the chloroplast, an observation that solves a long-standing paradox of central metabolism.
{"title":"Rubisco supplies pyruvate for the 2-C-methyl-d-erythritol-4-phosphate pathway","authors":"Sonia E. Evans, Yuan Xu, Matthew E. Bergman, Scott A. Ford, Yingxia Liu, Thomas D. Sharkey, Michael A. Phillips","doi":"10.1038/s41477-024-01791-z","DOIUrl":"10.1038/s41477-024-01791-z","url":null,"abstract":"RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (Rubisco) produces pyruvate in the chloroplast through β-elimination of the aci-carbanion intermediate1. Here we show that this side reaction supplies pyruvate for isoprenoid, fatty acid and branched-chain amino acid biosynthesis in photosynthetically active tissue. 13C labelling studies of intact Arabidopsis plants demonstrate that the total carbon commitment to pyruvate is too large for phosphoenolpyruvate to serve as a precursor. Low oxygen stimulates Rubisco carboxylase activity and increases pyruvate production and flux through the 2-C-methyl-d-erythritol-4-phosphate (MEP) pathway, which supplies the precursors for plastidic isoprenoid biosynthesis2,3. Metabolome analysis of mutants defective in phosphoenolpyruvate or pyruvate import and biochemical characterization of isolated chloroplasts further support Rubisco as the main source of pyruvate in chloroplasts. Seedlings incorporated exogenous,13C-labelled pyruvate into MEP pathway intermediates, while adult plants did not, underscoring the developmental transition in pyruvate sourcing. Rubisco β-elimination leading to pyruvate constituted 0.7% of the product profile in in vitro assays, which translates to 2% of the total carbon leaving the Calvin–Benson–Bassham cycle. These insights solve the “pyruvate paradox”4, improve the fit of metabolic models for central metabolism and connect the MEP pathway directly to carbon assimilation. As nature’s most important enzyme, Rubisco fixes carbon dioxide in the Calvin–Benson–Bassham cycle. Its lesser-known side job is supplying pyruvate in the chloroplast, an observation that solves a long-standing paradox of central metabolism.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 10","pages":"1453-1463"},"PeriodicalIF":15.8,"publicationDate":"2024-10-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142374125","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 : 2024-10-03DOI: 10.1038/s41477-024-01804-x
Sebastian Pintscher, Rafał Pietras, Bohun Mielecki, Mateusz Szwalec, Anna Wójcik-Augustyn, Paulina Indyka, Michał Rawski, Łukasz Koziej, Marcin Jaciuk, Grzegorz Ważny, Sebastian Glatt, Artur Osyczka
A multi-subunit enzyme, cytochrome b6f (cytb6f), provides the crucial link between photosystems I and II in the photosynthetic membranes of higher plants, transferring electrons between plastoquinone (PQ) and plastocyanin. The atomic structure of cytb6f is known, but its detailed catalytic mechanism remains elusive. Here we present cryogenic electron microscopy structures of spinach cytb6f at 1.9 Å and 2.2 Å resolution, revealing an unexpected orientation of the substrate PQ in the haem ligand niche that forms the PQ reduction site (Qn). PQ, unlike Qn inhibitors, is not in direct contact with the haem. Instead, a water molecule is coordinated by one of the carbonyl groups of PQ and can act as the immediate proton donor for PQ. In addition, we identify water channels that connect Qn with the aqueous exterior of the enzyme, suggesting that the binding of PQ in Qn displaces water through these channels. The structures confirm large movements of the head domain of the iron–sulfur protein (ISP-HD) towards and away from the plastoquinol oxidation site (Qp) and define the unique position of ISP-HD when a Qp inhibitor (2,5-dibromo-3-methyl-6-isopropylbenzoquinone) is bound. This work identifies key conformational states of cytb6f, highlights fundamental differences between substrates and inhibitors and proposes a quinone–water exchange mechanism. Cryo-EM structures of cytb6f with quinone bound in the Qn site allow the identification of specific proton channels and reveal differences to known inhibitors. Nearby water channels imply a ‘piston-like’ mechanism during catalytic turnover.
一种多亚基酶--细胞色素 b6f（cytb6f）--是高等植物光合膜中光合系统 I 和 II 之间的关键纽带，它在质醌（PQ）和质花青素之间传递电子。细胞b6f的原子结构已知，但其详细的催化机理仍不清楚。在这里，我们以 1.9 Å 和 2.2 Å 的分辨率展示了菠菜 cytb6f 的低温电子显微镜结构，揭示了底物 PQ 在形成 PQ 还原位点（Qn）的血红素配体位点中的意外取向。与 Qn 抑制剂不同，PQ 并不与血红素直接接触。相反，一个水分子与 PQ 的一个羰基配位，可作为 PQ 的直接质子供体。此外，我们还发现了连接 Qn 与酶的水外部的水通道，这表明 Qn 中 PQ 的结合会通过这些通道置换出水。这些结构证实了铁硫蛋白头部结构域（ISP-HD）向和远离质醌氧化位点（Qp）的大量运动，并确定了当 Qp 抑制剂（2,5-二溴-3-甲基-6-异丙基苯醌）结合时 ISP-HD 的独特位置。这项工作确定了细胞b6f的关键构象状态，突出了底物和抑制剂之间的根本差异，并提出了一种醌水交换机制。
{"title":"Molecular basis of plastoquinone reduction in plant cytochrome b6f","authors":"Sebastian Pintscher, Rafał Pietras, Bohun Mielecki, Mateusz Szwalec, Anna Wójcik-Augustyn, Paulina Indyka, Michał Rawski, Łukasz Koziej, Marcin Jaciuk, Grzegorz Ważny, Sebastian Glatt, Artur Osyczka","doi":"10.1038/s41477-024-01804-x","DOIUrl":"10.1038/s41477-024-01804-x","url":null,"abstract":"A multi-subunit enzyme, cytochrome b6f (cytb6f), provides the crucial link between photosystems I and II in the photosynthetic membranes of higher plants, transferring electrons between plastoquinone (PQ) and plastocyanin. The atomic structure of cytb6f is known, but its detailed catalytic mechanism remains elusive. Here we present cryogenic electron microscopy structures of spinach cytb6f at 1.9 Å and 2.2 Å resolution, revealing an unexpected orientation of the substrate PQ in the haem ligand niche that forms the PQ reduction site (Qn). PQ, unlike Qn inhibitors, is not in direct contact with the haem. Instead, a water molecule is coordinated by one of the carbonyl groups of PQ and can act as the immediate proton donor for PQ. In addition, we identify water channels that connect Qn with the aqueous exterior of the enzyme, suggesting that the binding of PQ in Qn displaces water through these channels. The structures confirm large movements of the head domain of the iron–sulfur protein (ISP-HD) towards and away from the plastoquinol oxidation site (Qp) and define the unique position of ISP-HD when a Qp inhibitor (2,5-dibromo-3-methyl-6-isopropylbenzoquinone) is bound. This work identifies key conformational states of cytb6f, highlights fundamental differences between substrates and inhibitors and proposes a quinone–water exchange mechanism. Cryo-EM structures of cytb6f with quinone bound in the Qn site allow the identification of specific proton channels and reveal differences to known inhibitors. Nearby water channels imply a ‘piston-like’ mechanism during catalytic turnover.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 11","pages":"1814-1825"},"PeriodicalIF":15.8,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.com/articles/s41477-024-01804-x.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369347","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 : 2024-10-02DOI: 10.1038/s41477-024-01819-4
Jessica Orozco, Paula Guzmán-Delgado, Maciej A. Zwieniecki
The global incidence of megafires is on the rise, leading to extensive areas being shrouded in dense smoke for prolonged periods, spanning days or weeks1. Here, by integrating long-term regional observations of non-structural carbohydrate content in trees across California’s Central Valley with spatiotemporal satellite data, we present compelling evidence that dense smoke plumes negatively impact carbohydrate stores in three tree species: Prunus dulcis, Pistacia vera and Juglans regia. Our findings show that the presence of smoke causes a significant decrease in total non-structural carbohydrates, with reductions in the accumulation of both soluble sugar and starch reserves. This decline in carbohydrate levels persists through the trees’ dormancy period into the next season’s bloom, culminating in a reduced yield. Our results highlight a previously unrecognized wildfire threat that could affect plant health and ecosystem stability in both agricultural and natural environments. The incidence and severity of megafires are increasing as a consequence of global change. While the impacts of fires on tree physiology and ecosystem functioning are well studied, how smoke affects these processes is less clear. Here Orozco et al. report that wildfire smoke significantly reduces tree carbohydrate reserves and yields, revealing an overlooked consequence of wildfires.
全球特大火灾的发生率正在上升，导致大片地区长时间笼罩在浓烟中，持续时间长达数天或数周1。在这里，通过将对加利福尼亚中央山谷树木非结构性碳水化合物含量的长期区域观测结果与时空卫星数据相结合，我们提出了令人信服的证据，证明浓烟对三种树木的碳水化合物储存产生了负面影响：Prunus dulcis、Pistacia vera 和 Juglans regia。我们的研究结果表明，烟雾的存在导致非结构性碳水化合物总量显著减少，可溶性糖和淀粉储备的积累也随之减少。这种碳水化合物水平的下降会持续到树木休眠期直至下一季开花，最终导致减产。我们的研究结果突显了一种以前未被认识到的野火威胁，它可能会影响农业和自然环境中的植物健康和生态系统稳定性。
{"title":"Megafire smoke exposure jeopardizes tree carbohydrate reserves and yield","authors":"Jessica Orozco, Paula Guzmán-Delgado, Maciej A. Zwieniecki","doi":"10.1038/s41477-024-01819-4","DOIUrl":"10.1038/s41477-024-01819-4","url":null,"abstract":"The global incidence of megafires is on the rise, leading to extensive areas being shrouded in dense smoke for prolonged periods, spanning days or weeks1. Here, by integrating long-term regional observations of non-structural carbohydrate content in trees across California’s Central Valley with spatiotemporal satellite data, we present compelling evidence that dense smoke plumes negatively impact carbohydrate stores in three tree species: Prunus dulcis, Pistacia vera and Juglans regia. Our findings show that the presence of smoke causes a significant decrease in total non-structural carbohydrates, with reductions in the accumulation of both soluble sugar and starch reserves. This decline in carbohydrate levels persists through the trees’ dormancy period into the next season’s bloom, culminating in a reduced yield. Our results highlight a previously unrecognized wildfire threat that could affect plant health and ecosystem stability in both agricultural and natural environments. The incidence and severity of megafires are increasing as a consequence of global change. While the impacts of fires on tree physiology and ecosystem functioning are well studied, how smoke affects these processes is less clear. Here Orozco et al. report that wildfire smoke significantly reduces tree carbohydrate reserves and yields, revealing an overlooked consequence of wildfires.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 11","pages":"1635-1642"},"PeriodicalIF":15.8,"publicationDate":"2024-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142362737","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 : 2024-09-30DOI: 10.1038/s41477-024-01806-9
Claudia Martinho
Genetic analysis has shown that RNA polymerase V (Pol V) regulates plant defence independently of its known function in RNA-directed DNA methylation. These findings reveal a mechanism whereby Pol V transcripts regulate gene expression upon infection with pathogens.
遗传分析表明，RNA聚合酶V（Pol V）除了具有已知的RNA定向DNA甲基化功能外，还能调节植物防御功能。这些发现揭示了 Pol V 转录物在病原体感染时调控基因表达的机制。
{"title":"From RdDM to plant defence","authors":"Claudia Martinho","doi":"10.1038/s41477-024-01806-9","DOIUrl":"10.1038/s41477-024-01806-9","url":null,"abstract":"Genetic analysis has shown that RNA polymerase V (Pol V) regulates plant defence independently of its known function in RNA-directed DNA methylation. These findings reveal a mechanism whereby Pol V transcripts regulate gene expression upon infection with pathogens.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 10","pages":"1442-1443"},"PeriodicalIF":15.8,"publicationDate":"2024-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142330338","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 : 2024-09-27DOI: 10.1038/s41477-024-01795-9
Huaxun Ye, Mei Louden, Jon A. T. Reinders
Doubled haploid (DH) technologies accelerate maize inbred development. Recently, methods using CRISPR–Cas have created gene-edited maize DH populations, albeit with relatively low editing frequencies. Restoring fertility via haploid chromosome doubling remains a critically important production constraint. Thus, improved editing and chromosome doubling outcomes are needed. Here we obtained maternally derived diploid embryos in vivo by ectopically co-expressing Zea mays BABY BOOM and cyclin D-like gene products within unfertilized egg cells. When combined with gene editing, the in vivo method enables the production of mature seed with a maternally derived, gene-edited diploid embryo without requiring in vitro tissue culture methods nor the use of a chemical chromosome doubling agent. In summary, we report a novel approach for creating gene-edited maize DH populations that we expect can accelerate genetic gain in a scalable, cost-effective manner. Ye et al. use a novel genetic haploid genome doubling method with parthenogenesis and gene editing to produce edited, maternally derived di-haploid progeny. A truncated BABY BOOM peptide confers both parthenogenesis and haploid genome doubling.
{"title":"A novel in vivo genome editing doubled haploid system for Zea mays L.","authors":"Huaxun Ye, Mei Louden, Jon A. T. Reinders","doi":"10.1038/s41477-024-01795-9","DOIUrl":"10.1038/s41477-024-01795-9","url":null,"abstract":"Doubled haploid (DH) technologies accelerate maize inbred development. Recently, methods using CRISPR–Cas have created gene-edited maize DH populations, albeit with relatively low editing frequencies. Restoring fertility via haploid chromosome doubling remains a critically important production constraint. Thus, improved editing and chromosome doubling outcomes are needed. Here we obtained maternally derived diploid embryos in vivo by ectopically co-expressing Zea mays BABY BOOM and cyclin D-like gene products within unfertilized egg cells. When combined with gene editing, the in vivo method enables the production of mature seed with a maternally derived, gene-edited diploid embryo without requiring in vitro tissue culture methods nor the use of a chemical chromosome doubling agent. In summary, we report a novel approach for creating gene-edited maize DH populations that we expect can accelerate genetic gain in a scalable, cost-effective manner. Ye et al. use a novel genetic haploid genome doubling method with parthenogenesis and gene editing to produce edited, maternally derived di-haploid progeny. A truncated BABY BOOM peptide confers both parthenogenesis and haploid genome doubling.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 10","pages":"1493-1501"},"PeriodicalIF":15.8,"publicationDate":"2024-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142325579","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 : 2024-09-27DOI: 10.1038/s41477-024-01807-8
Mathieu Raingeval, Basile Leduque, Pierre Baduel, Alejandro Edera, Fabrice Roux, Vincent Colot, Leandro Quadrana
The mobilization of transposable elements is a potent source of mutations. In plants, several stransposable elements respond to external cues, fuelling the hypothesis that natural transposition can create environmentally sensitive alleles for adaptation. Here we report on the detailed characterization of a retrotransposon insertion within the first intron of the Arabidopsis floral-repressor gene FLOWERING LOCUS C (FLC) and the discovery of its role for adaptation. The insertion mutation augments the environmental sensitivity of FLC by affecting the balance between coding and non-coding transcripts in response to stress, thus expediting flowering. This balance is modulated by DNA methylation and orchestrated by IBM2, a factor involved in the processing of intronic heterochromatic sequences. The stress-sensitive allele of FLC has spread across populations subjected to recurrent chemical weeding, and we show that retrotransposon-driven acceleration of the life cycle represents a rapid response to herbicide application. Our work provides a compelling example of a transposable element-driven environmentally sensitive allele that confers an adaptive response in nature. This study reports the discovery of a retrotransposon insertion in the FLC gene conferring an environmentally dependent control mechanism mediated by DNA methylation that drives the adaptation of natural Arabidopsis populations to herbicide exposure.
转座元件的调动是突变的强大来源。在植物中，一些可转座元件会对外界线索做出反应，从而推动了自然转座可产生对环境敏感的等位基因以适应环境的假说。在这里，我们报告了拟南芥花卉抑制基因 FLOWERING LOCUS C（FLC）第一个内含子中一个逆转录转座子插入的详细特征，并发现了它在适应中的作用。插入突变通过影响编码转录本和非编码转录本之间的平衡来提高 FLC 对环境的敏感性，从而加速开花。这种平衡由 DNA 甲基化调节，并由 IBM2（一种参与处理内含子异染色质序列的因子）协调。FLC 的胁迫敏感等位基因已在经常进行化学除草的种群中扩散，我们的研究表明，逆转录转座子驱动的生命周期加速是对除草剂应用的快速反应。我们的工作为转座元件驱动的环境敏感等位基因在自然界中赋予适应性反应提供了一个令人信服的例子。
{"title":"Retrotransposon-driven environmental regulation of FLC leads to adaptive response to herbicide","authors":"Mathieu Raingeval, Basile Leduque, Pierre Baduel, Alejandro Edera, Fabrice Roux, Vincent Colot, Leandro Quadrana","doi":"10.1038/s41477-024-01807-8","DOIUrl":"10.1038/s41477-024-01807-8","url":null,"abstract":"The mobilization of transposable elements is a potent source of mutations. In plants, several stransposable elements respond to external cues, fuelling the hypothesis that natural transposition can create environmentally sensitive alleles for adaptation. Here we report on the detailed characterization of a retrotransposon insertion within the first intron of the Arabidopsis floral-repressor gene FLOWERING LOCUS C (FLC) and the discovery of its role for adaptation. The insertion mutation augments the environmental sensitivity of FLC by affecting the balance between coding and non-coding transcripts in response to stress, thus expediting flowering. This balance is modulated by DNA methylation and orchestrated by IBM2, a factor involved in the processing of intronic heterochromatic sequences. The stress-sensitive allele of FLC has spread across populations subjected to recurrent chemical weeding, and we show that retrotransposon-driven acceleration of the life cycle represents a rapid response to herbicide application. Our work provides a compelling example of a transposable element-driven environmentally sensitive allele that confers an adaptive response in nature. This study reports the discovery of a retrotransposon insertion in the FLC gene conferring an environmentally dependent control mechanism mediated by DNA methylation that drives the adaptation of natural Arabidopsis populations to herbicide exposure.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 11","pages":"1672-1681"},"PeriodicalIF":15.8,"publicationDate":"2024-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142329015","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 : 2024-09-27DOI: 10.1038/s41477-024-01792-y
Marco Catoni
The insertion of the stress-responsive transposable element (TE) ONSEN into a critical flowering regulator gene confers an adaptive response to herbicide treatment in Arabidopsis thaliana natural accessions.
{"title":"Transposable elements underlie genetic adaptation","authors":"Marco Catoni","doi":"10.1038/s41477-024-01792-y","DOIUrl":"10.1038/s41477-024-01792-y","url":null,"abstract":"The insertion of the stress-responsive transposable element (TE) ONSEN into a critical flowering regulator gene confers an adaptive response to herbicide treatment in Arabidopsis thaliana natural accessions.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 11","pages":"1617-1618"},"PeriodicalIF":15.8,"publicationDate":"2024-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142325577","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}
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