The nervous system must coordinate complex ensembles of electrical activity across great distances. To achieve this, specialized cells in the central nervous system called oligodendrocytes wrap the axons of neurons in an insulating membrane called myelin. Myelin increases the conduction velocity of electrical impulses and provides important metabolic support to the ensheathed axons (1). Because of these properties, myelination is critical for cognition, memory, movement, and perception. Myelin loss in disease states can cause severe neurological symptoms; however, the physiology underlying how various insults eventually progress to demyelination in disease contexts had not been well characterized in the central nervous system. On page 686 of this issue, Arafa et al. (2) report that damage to myelin initially causes swelling before leading to loss of myelin sheaths. They also demonstrate that swollen myelin can persist despite damage and can dynamically remodel to prevent sheath loss.
{"title":"Rest to repair","authors":"Kamsi Nwangwu, Michelle Monje","doi":"10.1126/science.aef0057","DOIUrl":"10.1126/science.aef0057","url":null,"abstract":"<div >The nervous system must coordinate complex ensembles of electrical activity across great distances. To achieve this, specialized cells in the central nervous system called oligodendrocytes wrap the axons of neurons in an insulating membrane called myelin. Myelin increases the conduction velocity of electrical impulses and provides important metabolic support to the ensheathed axons (<i>1</i>). Because of these properties, myelination is critical for cognition, memory, movement, and perception. Myelin loss in disease states can cause severe neurological symptoms; however, the physiology underlying how various insults eventually progress to demyelination in disease contexts had not been well characterized in the central nervous system. On page 686 of this issue, Arafa <i>et al</i>. (<i>2</i>) report that damage to myelin initially causes swelling before leading to loss of myelin sheaths. They also demonstrate that swollen myelin can persist despite damage and can dynamically remodel to prevent sheath loss.</div>","PeriodicalId":21678,"journal":{"name":"Science","volume":"391 6786","pages":""},"PeriodicalIF":45.8,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146162944","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Donghwi Ko, Raili Ruonala, Alexandre Faille, Eva Hellmann, Hanna Help, Huili Liu, Ronni Nielsen, Anders Haakonsson, Nuria De Diego, Anja Paatero, Mariia V. Shcherbii, Karolina Stefanowicz, Sanja Ćavar Zeljković, Tine Drud Lundager Rasmussen, Ondrej Novak, Zsuzsanna Bodi, Gugan Eswaran, Brecht Wybouw, Matthieu Bourdon, Cristina Urbez, Xiaonan Liu, Kari Salokas, Tiina Öhman, Tanya Waldie, Petri Törönen, Sedeer el-Showk, Martin Balcerowicz, Fabrice Besnard, Xiaomin Liu, Patrick Perkins, Serina Mazzoni-Putman, Julia P. Vainonen, Maija Sierla, Mikko J. Frilander, Susanne Mandrup, Teva Vernoux, Karin Ljung, Alejandro Ferrando, Miguel A. Blazquez, Liisa Holm, Rupert Fray, Markku Varjosalo, Ottoline Leyser, Ville O. Paavilainen, Ari Pekka Mähönen, Anna Stepanova, Jose Alonso, Steffen Heber, Robert Malinowski, Finn Kirpekar, Alan J. Warren, Ykä Helariutta
Polyamines are often associated with ribosomes and are thought to stabilize their integrity. In Arabidopsis, the polyamine thermospermine (tSpm) affects xylem cell fate. tSpm induces translation of SUPPRESSOR-OF-ACAULIS51 (SAC51) and SAC51-LIKEs (SACLs), which inhibit heterodimerization of the xylem development proteins LONESOME-HIGHWAY (LHW) and TARGET-OF-MONOPTEROS5. Here, we report a methyltransferase, OVERACHIEVER, that methylates the peptidyl transferase center of the 25S ribosomal RNA (rRNA). Residue m3U2952 promotes functional tSpm binding to a specific site connecting the P-site transfer RNA (tRNA) with rRNA residues in the peptidyl transferase center. This interaction enhances the translation of SACLs but inhibits that of LHW. Our study uncovers the dependency between a conserved rRNA base methylation and a polyamine in orchestrating cell fate decisions, highlighting a role for the ribosome chemical landscape in translational regulation.
多胺常与核糖体结合，被认为能稳定核糖体的完整性。在拟南芥中，多胺热精胺（tSpm）影响木质部细胞命运。tSpm诱导acaulis51 SUPPRESSOR-OF-ACAULIS51 （SAC51）和SAC51- like （SACLs）的翻译，从而抑制木质部发育蛋白LONESOME-HIGHWAY （LHW）和TARGET-OF-MONOPTEROS5的异源二聚化。在这里，我们报道了一种甲基转移酶OVERACHIEVER，它使25S核糖体RNA （rRNA）的肽基转移酶中心甲基化。残基m3U2952促进功能性tSpm与肽基转移酶中心连接p -位点转移RNA （tRNA）和rRNA残基的特定位点结合。这种相互作用增强了sacl的翻译，抑制了LHW的翻译。我们的研究揭示了保守的rRNA碱基甲基化和多胺在协调细胞命运决定中的依赖关系，强调了核糖体化学景观在翻译调节中的作用。
{"title":"Recruitment of bifunctional regulator thermospermine to methylated ribosomes directs xylem fate","authors":"Donghwi Ko, Raili Ruonala, Alexandre Faille, Eva Hellmann, Hanna Help, Huili Liu, Ronni Nielsen, Anders Haakonsson, Nuria De Diego, Anja Paatero, Mariia V. Shcherbii, Karolina Stefanowicz, Sanja Ćavar Zeljković, Tine Drud Lundager Rasmussen, Ondrej Novak, Zsuzsanna Bodi, Gugan Eswaran, Brecht Wybouw, Matthieu Bourdon, Cristina Urbez, Xiaonan Liu, Kari Salokas, Tiina Öhman, Tanya Waldie, Petri Törönen, Sedeer el-Showk, Martin Balcerowicz, Fabrice Besnard, Xiaomin Liu, Patrick Perkins, Serina Mazzoni-Putman, Julia P. Vainonen, Maija Sierla, Mikko J. Frilander, Susanne Mandrup, Teva Vernoux, Karin Ljung, Alejandro Ferrando, Miguel A. Blazquez, Liisa Holm, Rupert Fray, Markku Varjosalo, Ottoline Leyser, Ville O. Paavilainen, Ari Pekka Mähönen, Anna Stepanova, Jose Alonso, Steffen Heber, Robert Malinowski, Finn Kirpekar, Alan J. Warren, Ykä Helariutta","doi":"10.1126/science.adx2867","DOIUrl":"10.1126/science.adx2867","url":null,"abstract":"<div >Polyamines are often associated with ribosomes and are thought to stabilize their integrity. In <i>Arabidopsis</i>, the polyamine thermospermine (tSpm) affects xylem cell fate. tSpm induces translation of SUPPRESSOR-OF-ACAULIS51 (SAC51) and SAC51-LIKEs (SACLs), which inhibit heterodimerization of the xylem development proteins LONESOME-HIGHWAY (LHW) and TARGET-OF-MONOPTEROS5. Here, we report a methyltransferase, OVERACHIEVER, that methylates the peptidyl transferase center of the 25<i>S</i> ribosomal RNA (rRNA). Residue m<sup>3</sup>U2952 promotes functional tSpm binding to a specific site connecting the P-site transfer RNA (tRNA) with rRNA residues in the peptidyl transferase center. This interaction enhances the translation of SACLs but inhibits that of LHW. Our study uncovers the dependency between a conserved rRNA base methylation and a polyamine in orchestrating cell fate decisions, highlighting a role for the ribosome chemical landscape in translational regulation.</div>","PeriodicalId":21678,"journal":{"name":"Science","volume":"391 6786","pages":""},"PeriodicalIF":45.8,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146162947","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Erratum for the Research Article “Of the first five US states with food waste bans, Massachusetts alone has reduced landfill waste”","authors":"","doi":"10.1126/science.aef7764","DOIUrl":"10.1126/science.aef7764","url":null,"abstract":"","PeriodicalId":21678,"journal":{"name":"Science","volume":"391 6786","pages":""},"PeriodicalIF":45.8,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146162953","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Han P Q Nguyen, Alexander J Maertens, Benjamin A Baker, Nathan M-W Wu, Zihao Ye, Qingyang Zhou, Qianfeng Qiu, Navneet Kaur, David B Berkinsky, Katherine E Shulenberger, K N Houk, Grace G D Han
Storing sunlight in a compact and rechargeable form remains a central challenge for solar energy utilization. Molecular solar thermal (MOST) energy storage systems, which harness photon energy and release it as heat on demand, provide a direct approach, but have long failed to meet practical benchmarks. Inspired by the architecture of DNA, we report a pyrimidone-based MOST system that stores energy in the strained Dewar photoisomer upon excitation at 300 nm. Designed with sustainability in mind, the system operates solvent-free and remains compatible with aqueous environments while overcoming one of the field's greatest hurdles: the controlled extraction and transfer of stored heat. When catalyzed by acid, the Dewar isomer releases enough heat to boil water (~0.5 mL). These advances help point the way toward decentralized solar heat storage and off-grid energy solutions.
{"title":"Molecular solar thermal energy storage in Dewar pyrimidone beyond 1.6 MJ/kg.","authors":"Han P Q Nguyen, Alexander J Maertens, Benjamin A Baker, Nathan M-W Wu, Zihao Ye, Qingyang Zhou, Qianfeng Qiu, Navneet Kaur, David B Berkinsky, Katherine E Shulenberger, K N Houk, Grace G D Han","doi":"10.1126/science.aec6413","DOIUrl":"https://doi.org/10.1126/science.aec6413","url":null,"abstract":"<p><p>Storing sunlight in a compact and rechargeable form remains a central challenge for solar energy utilization. Molecular solar thermal (MOST) energy storage systems, which harness photon energy and release it as heat on demand, provide a direct approach, but have long failed to meet practical benchmarks. Inspired by the architecture of DNA, we report a pyrimidone-based MOST system that stores energy in the strained Dewar photoisomer upon excitation at 300 nm. Designed with sustainability in mind, the system operates solvent-free and remains compatible with aqueous environments while overcoming one of the field's greatest hurdles: the controlled extraction and transfer of stored heat. When catalyzed by acid, the Dewar isomer releases enough heat to boil water (~0.5 mL). These advances help point the way toward decentralized solar heat storage and off-grid energy solutions.</p>","PeriodicalId":21678,"journal":{"name":"Science","volume":" ","pages":"eaec6413"},"PeriodicalIF":45.8,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146182068","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Geopolitics cast shadow over preparations for 2032 effort to study poles.
地缘政治给2032年研究极地的准备工作蒙上了阴影。
{"title":"Polar Year plans heat up.","authors":"Richard Stone","doi":"10.1126/science.aeg3561","DOIUrl":"https://doi.org/10.1126/science.aeg3561","url":null,"abstract":"<p><p>Geopolitics cast shadow over preparations for 2032 effort to study poles.</p>","PeriodicalId":21678,"journal":{"name":"Science","volume":"391 6786","pages":"648-649"},"PeriodicalIF":45.8,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146182098","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Oregon university votes to explore NIH offer to transform national facility.
俄勒冈大学投票决定探索国立卫生研究院改造国家设施的提议。
{"title":"Giant primate research center may become sanctuary.","authors":"David Grimm","doi":"10.1126/science.aeg3557","DOIUrl":"https://doi.org/10.1126/science.aeg3557","url":null,"abstract":"<p><p>Oregon university votes to explore NIH offer to transform national facility.</p>","PeriodicalId":21678,"journal":{"name":"Science","volume":"391 6786","pages":"642-643"},"PeriodicalIF":45.8,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146182116","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Simon Greenhill, Solomon Hsiang, Clare Balboni, Lint Barrage, Ian W. Bolliger, Judson Boomhower, Delavane Diaz, Hannah Druckenmiller, Teevrat Garg, Miyuki Hino, Harrison Hong, Carolyn Kousky, Jeremy Martinich, Ishan Nath, Kimberly L. Oremus, R. Jisung Park, Toan Phan, Jonathan Proctor, Will Rafey, Marcus C. Sarofim, Wolfram Schlenker, Benjamin Simon
Even under the most ambitious greenhouse gas emissions mitigation scenarios, climate change will continue to affect human well-being for generations, with the severity of these impacts differing across mitigation pathways. Adapting to climate change is thus a necessary complement to mitigation. Because individuals, businesses, and communities benefit directly from their adaptation choices, the incentives they face as individuals to adapt are generally stronger than the incentives they face to mitigate emissions. Yet evidence to date suggests that communities are not systematically adapting to recent climate changes (1). What can policy-makers do to facilitate adaptation? Here, we draw on a burgeoning field of economic research on climate adaptation to identify when and how markets can be a promising tool for effective and efficient adaptation.
{"title":"Using markets to adapt to climate change","authors":"Simon Greenhill, Solomon Hsiang, Clare Balboni, Lint Barrage, Ian W. Bolliger, Judson Boomhower, Delavane Diaz, Hannah Druckenmiller, Teevrat Garg, Miyuki Hino, Harrison Hong, Carolyn Kousky, Jeremy Martinich, Ishan Nath, Kimberly L. Oremus, R. Jisung Park, Toan Phan, Jonathan Proctor, Will Rafey, Marcus C. Sarofim, Wolfram Schlenker, Benjamin Simon","doi":"10.1126/science.aea7431","DOIUrl":"10.1126/science.aea7431","url":null,"abstract":"<div >Even under the most ambitious greenhouse gas emissions mitigation scenarios, climate change will continue to affect human well-being for generations, with the severity of these impacts differing across mitigation pathways. Adapting to climate change is thus a necessary complement to mitigation. Because individuals, businesses, and communities benefit directly from their adaptation choices, the incentives they face as individuals to adapt are generally stronger than the incentives they face to mitigate emissions. Yet evidence to date suggests that communities are not systematically adapting to recent climate changes (<i>1</i>). What can policy-makers do to facilitate adaptation? Here, we draw on a burgeoning field of economic research on climate adaptation to identify when and how markets can be a promising tool for effective and efficient adaptation.</div>","PeriodicalId":21678,"journal":{"name":"Science","volume":"391 6786","pages":""},"PeriodicalIF":45.8,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146162951","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Many plant pathogenic fungi penetrate host surfaces mechanically, using turgor pressure generated by specialized infection cells called appressoria. These appressoria develop semipermeable cell walls and accumulate osmolytes internally to create turgor by osmosis. Although melanin is known to be important for turgor generation, the mechanism underlying wall semipermeability remains unclear. By using reverse genetics, we identified that the enzymes PKS2 and PBG13 are required for forming the semipermeable barrier in fungi causing anthracnose and rice blast diseases. These enzymes synthesize 3,5-dihydroxyhexanoic acid polymers that are essential for pathogenicity. These polymers reduce cell wall permeability and generate turgor, independently of melanization. Our findings uncover a mechanism of fungal turgor generation, linking enzyme function to pathogen penetration and disease potential, presenting new targets for disease control.
{"title":"Dihydroxyhexanoic acid biosynthesis controls turgor in pathogenic fungi","authors":"Naoyoshi Kumakura, Takayuki Motoyama, Keisuke Miyazawa, Toshihiko Nogawa, Julien Pernier, Katsuma Yonehara, Mayuko Sato, Yumi Goto, Kaori Sakai, Nobuaki Ishihama, Kaisei Matsumori, Pamela Gan, Kiminori Toyooka, Sandrine Lévêque-Fort, Hiroyuki Koshino, Takeshi Fukuma, Richard J. O’Connell, Ken Shirasu","doi":"10.1126/science.aec9443","DOIUrl":"10.1126/science.aec9443","url":null,"abstract":"<div >Many plant pathogenic fungi penetrate host surfaces mechanically, using turgor pressure generated by specialized infection cells called appressoria. These appressoria develop semipermeable cell walls and accumulate osmolytes internally to create turgor by osmosis. Although melanin is known to be important for turgor generation, the mechanism underlying wall semipermeability remains unclear. By using reverse genetics, we identified that the enzymes PKS2 and PBG13 are required for forming the semipermeable barrier in fungi causing anthracnose and rice blast diseases. These enzymes synthesize 3,5-dihydroxyhexanoic acid polymers that are essential for pathogenicity. These polymers reduce cell wall permeability and generate turgor, independently of melanization. Our findings uncover a mechanism of fungal turgor generation, linking enzyme function to pathogen penetration and disease potential, presenting new targets for disease control.</div>","PeriodicalId":21678,"journal":{"name":"Science","volume":"391 6786","pages":""},"PeriodicalIF":45.8,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146162960","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Aerin Yang, Hanlun Jiang, Kevin M. Jude, Deniz Akpinaroglu, Stephan Allenspach, Alex Jie Li, James Bowden, Carla Patricia Perez, Liu Liu, Po-Ssu Huang, Tanja Kortemme, Jennifer Listgarten, K. Christopher Garcia
Understanding how protein binding sites evolve interactions with other proteins could hold clues to targeting “undruggable” surfaces. We used synthetic coevolution to engineer new interactions between naïve surfaces, simulating the de novo formation of protein complexes. We isolated seven distinct structural families of protein Z-domain complexes and found that synthetic complexes explore multiple shallow energy wells through ratchet-like docking modes, whereas complexes formed by natural binding sites converged in a deep energy well with a relatively fixed geometry. Epistasis analysis of a machine learning–estimated fitness landscape revealed “seed” contacts between binding partners that anchored the earliest stages of encounter complex formation. Our results suggest that “silent” surfaces have a shallower energy landscape than natural binding sites, disfavoring tight binding, likely owing to evolutionary counterselection.
{"title":"Structural ontogeny of protein-protein interactions","authors":"Aerin Yang, Hanlun Jiang, Kevin M. Jude, Deniz Akpinaroglu, Stephan Allenspach, Alex Jie Li, James Bowden, Carla Patricia Perez, Liu Liu, Po-Ssu Huang, Tanja Kortemme, Jennifer Listgarten, K. Christopher Garcia","doi":"10.1126/science.adx6931","DOIUrl":"10.1126/science.adx6931","url":null,"abstract":"<div >Understanding how protein binding sites evolve interactions with other proteins could hold clues to targeting “undruggable” surfaces. We used synthetic coevolution to engineer new interactions between naïve surfaces, simulating the de novo formation of protein complexes. We isolated seven distinct structural families of protein Z-domain complexes and found that synthetic complexes explore multiple shallow energy wells through ratchet-like docking modes, whereas complexes formed by natural binding sites converged in a deep energy well with a relatively fixed geometry. Epistasis analysis of a machine learning–estimated fitness landscape revealed “seed” contacts between binding partners that anchored the earliest stages of encounter complex formation. Our results suggest that “silent” surfaces have a shallower energy landscape than natural binding sites, disfavoring tight binding, likely owing to evolutionary counterselection.</div>","PeriodicalId":21678,"journal":{"name":"Science","volume":"391 6786","pages":""},"PeriodicalIF":45.8,"publicationDate":"2026-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146162940","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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