Nature PlantsPub Date : 2025-06-27DOI: 10.1038/s41477-025-02030-9
Chao Feng, Jana Lorenz, Steven Dreissig, Veit Schubert, Baicui Wang, Franziska Hartmann, Maria Cuacos, Nadia Fernández-Jiménez, Ziliang Zhao, Christian Eggeling, Amanda Souza Câmara, Axel Himmelbach, Stefan Heckmann
{"title":"The synaptonemal complex central element SCEP3 interlinks synapsis initiation and crossover formation in Arabidopsis thaliana","authors":"Chao Feng, Jana Lorenz, Steven Dreissig, Veit Schubert, Baicui Wang, Franziska Hartmann, Maria Cuacos, Nadia Fernández-Jiménez, Ziliang Zhao, Christian Eggeling, Amanda Souza Câmara, Axel Himmelbach, Stefan Heckmann","doi":"10.1038/s41477-025-02030-9","DOIUrl":"10.1038/s41477-025-02030-9","url":null,"abstract":"The synaptonemal complex (SC) forms between homologous chromosomes during meiosis. In Arabidopsis thaliana, its central region (CR) is composed of the transverse filament protein ZYP1 and the central element proteins SCEP1 and SCEP2. Here we identify SCEP3 as a CR protein that is evolutionarily conserved across plant species. SCEP3 spatiotemporally overlaps with other CR proteins and localizes to the SC CR. The loss of SCEP3 prevents SC assembly, abolishes crossover (CO) assurance and interference, and eliminates sex-specific differences in CO rates (heterochiasmy) through increased CO in females. SCEP3 is required for a subset of COs in SC-deficient mutants, such as zyp1. Although SCEP3 physically interacts with ZYP1, it loads independently of other CR proteins. We propose that SCEP3 may associate with certain recombination intermediates, stabilizing them and/or recruiting additional factors, such as ZYP1, to a subset of these intermediates, thereby promoting and interlinking SC assembly and CO formation. This study identifies SCEP3 as a conserved central element of the plant synaptonemal complex. SCEP3 is critical for synapsis, heterochiasmy and crossover interference. SCEP3 also promotes a subset of crossover events.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 7","pages":"1353-1366"},"PeriodicalIF":13.6,"publicationDate":"2025-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41477-025-02030-9.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144500544","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}
Nature PlantsPub Date : 2025-06-27DOI: 10.1038/s41477-025-02036-3
Yidi Wang, Chenxi Wang, Anjie Li, Zhenfeng Liu
{"title":"Roles of multiple TEF30-associated intermediate complexes in the repair and reassembly of photosystem II in Chlamydomonas reinhardtii","authors":"Yidi Wang, Chenxi Wang, Anjie Li, Zhenfeng Liu","doi":"10.1038/s41477-025-02036-3","DOIUrl":"10.1038/s41477-025-02036-3","url":null,"abstract":"During oxygenic photosynthesis, photosystem II (PSII) uses light energy for oxidizing water and reducing plastoquinone. It is susceptible to photodamage, and the damaged PSII is repaired through a sophisticated biological process assisted by numerous auxiliary proteins. Here we report the cryogenic electron microscopy structures of four PSII-repair complexes from Chlamydomonas reinhardtii associated with the Thylakoid Enriched Fraction 30 (TEF30, an orthologue of plant MET1) protein—namely, a TEF30–PSII core monomer (TEF30-C), two types of TEF30–PSII core dimers (types I and II, TEF302-C2-I and TEF302-C2-II) and a TEF30-C2S-type PSII–LHCII supercomplex (TEF30-C2S; S, strongly associated light-harvesting complex II trimer). TEF30 mediates the assembly of CP43 with the RC47 module by clamping on the stromal surfaces and prevents the premature association of peripheral antennae with PSII-C. In the transition from TEF302-C2-I to TEF302-C2-II, TEF30-C2S and mature C2S2, one PSII core slides along the dimerization interface against the adjacent one by 22–35 Å, generating a zigzagged surface for accommodating the peripheral antennae. These results suggest that the PSII repair process undergoes multiple TEF30-mediated intermediate states to form intact PSII–LHCII supercomplexes. Cryo-EM structures of four TEF30-associated photosystem II repair complexes from Chlamydomonas reinhardtii reveal versatile roles of TEF30 in the reassembly of the photosystem II core monomer, dimer and supercomplex through multiple intermediate states.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 7","pages":"1455-1469"},"PeriodicalIF":13.6,"publicationDate":"2025-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144500541","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}
Nature PlantsPub Date : 2025-06-27DOI: 10.1038/s41477-025-02034-5
Xiuyue Zhang, Minze Li, Xiaoyan Zhang, Rong Zeng, Yue Peng, Yiting Shi, Xiangfeng Wang, Wenkun Zhou, Zhizhong Gong, Shuhua Yang
{"title":"A receptor–kinase cascade confers cold-induced root growth inhibition in Arabidopsis","authors":"Xiuyue Zhang, Minze Li, Xiaoyan Zhang, Rong Zeng, Yue Peng, Yiting Shi, Xiangfeng Wang, Wenkun Zhou, Zhizhong Gong, Shuhua Yang","doi":"10.1038/s41477-025-02034-5","DOIUrl":"10.1038/s41477-025-02034-5","url":null,"abstract":"Cold stress restricts root growth by disrupting stem cell activity in plants. C-REPEAT BINDING FACTORs (CBFs) are central regulators of cold signalling and also modulate root stem cell activity. While the receptor-like cytoplasmic kinase CRPK1 promotes CBF destabilization under cold stress, its regulatory partner remains unclear. Here we identify KINASE ON THE INSIDE (KOIN), a plasma-membrane-localized receptor-like kinase, as a crucial interactor of CRPK1. The loss of either KOIN or CRPK1 results in cold-insensitive root phenotypes, characterized by sustained primary root elongation and enhanced cortex cell proliferation via the 14-3-3–CBF3–SHR pathway. Under cold stress, KOIN undergoes endocytosis and is recycled back to the plasma membrane in a CRPK1-dependent manner. Although catalytically inactive, KOIN modulates CRPK1 protein levels and phosphorylation through a non-catalytic mechanism. These findings uncover a membrane-to-nucleus signalling module that integrates receptor trafficking with intracellular kinase activity to mediate cold-induced root growth inhibition in Arabidopsis. A receptor–kinase module involving KOIN and CRPK1 integrates membrane trafficking and kinase signalling to mediate cold-induced root growth inhibition in Arabidopsis via the 14-3-3–CBF3–SHR pathway.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 7","pages":"1441-1454"},"PeriodicalIF":13.6,"publicationDate":"2025-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144500543","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}
{"title":"Transgene- and tissue culture-free heritable genome editing using RNA virus-based delivery in wheat","authors":"Ji-Hui Qiao, Ying Zang, Qiang Gao, Shengnan Liu, Xin-Wen Zhang, Weiyao Hu, Ying Wang, Chenggui Han, Dawei Li, Xian-Bing Wang","doi":"10.1038/s41477-025-02023-8","DOIUrl":"10.1038/s41477-025-02023-8","url":null,"abstract":"CRISPR–Cas genome editing technology is a cutting-edge strategy for crop breeding. However, the delivery of genome-editing reagents remains to be a technological bottleneck in monocot plants1. Here we engineered barley yellow striate mosaic virus (BYSMV) into a negative-strand RNA virus-based vector system2 for delivery of both Cas9 and single guide RNA to achieve heritable gene editing in different wheat cultivars. We found that fusion of a mobile transfer RNA sequence3 to the Cas9 messenger RNA and single guide RNAs could deliver them into the growth points of axillary meristems to achieve gene editing before tiller generation. The resulting nascent tillers contained simultaneous mutations in the three homoeoalleles. Moreover, the progeny seedlings are virus-free and harbour bi-allelic or homozygous mutations. Given BYSMV infects 26 monocot species4, the BYSMV delivery system could have wide applicability for achieving highly efficient, non-transgenic and less genotype-dependent heritable genome editing, thereby facilitating genomic studies and crops breeding. Efficient delivery systems are urgently needed for genome editing in monocot plants. Here, this study develops a system of virus-induced genome editing in tillers (ViGET) to achieve heritable editing in wheat bypassing transgene and tissue culture.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 7","pages":"1252-1259"},"PeriodicalIF":13.6,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144478961","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}
Nature PlantsPub Date : 2025-06-25DOI: 10.1038/s41477-025-02018-5
{"title":"Dynamic sex chromosome evolution in hops","authors":"","doi":"10.1038/s41477-025-02018-5","DOIUrl":"10.1038/s41477-025-02018-5","url":null,"abstract":"Using whole-genome sequences of cultivated and wild hops, we describe the evolution of sex chromosomes, including degeneration and dosage compensation, and identify a candidate gene for the X–autosome (X–A) balance sex-determination system in hops.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 7","pages":"1235-1236"},"PeriodicalIF":13.6,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144479079","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}
Nature PlantsPub Date : 2025-06-25DOI: 10.1038/s41477-025-02025-6
Abraham R. Steinberger, Daniel F. Voytas
{"title":"Virus-induced gene editing free from tissue culture","authors":"Abraham R. Steinberger, Daniel F. Voytas","doi":"10.1038/s41477-025-02025-6","DOIUrl":"10.1038/s41477-025-02025-6","url":null,"abstract":"Virus-induced gene editing (VIGE) has reached an inflection point. Although conceived as an alternative to traditional methods of producing gene-edited plants, VIGE has historically relied on the very technologies it was meant to supersede—specifically, tissue-culture-mediated transgenesis. Recent VIGE innovations, however, have finally proved its viability as an independent method for plant gene editing. Here we discuss the advances in plant genome engineering VIGE may unlock, what progress has been made towards achieving these advances and the challenges that continue to impede that progress. Recent advances have brought virus-induced gene editing closer to achieving its promise to simplify and democratize plant gene editing by weaning it from its dependence on tissue-culture-based transformation.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 7","pages":"1241-1251"},"PeriodicalIF":13.6,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144478953","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}
{"title":"PEN1 catalyses RNA primer removal during plastid DNA replication in maize","authors":"Xing Huang, Guolong Shi, Qiao Xiao, Jiaojiao Feng, Yongcai Huang, Hai Shi, Qiong Wang, Yu Su, Jiechen Wang, Xingguo Wu, Yuwei Cao, Haihai Wang, Wenqin Wang, Yu Zhang, Yongrui Wu","doi":"10.1038/s41477-025-02027-4","DOIUrl":"10.1038/s41477-025-02027-4","url":null,"abstract":"The plastid DNA (ptDNA) replication is initiated by primases, which synthesize RNA primers; following the synthesis of DNA fragments, primers must be removed before ligation. However, the enzymes and mechanisms underlying this process are poorly understood. Here we cloned a gene from maize that encodes a plastid-localized and Mn2+-dependent 5′–3′ exonuclease (designated PEN1) responsible for this process. The pen1 seeds show development and filling defects that intensify across generations. PEN1 cleaves the RNA primers, allowing for the complete excision of ribonucleotides. We reconstituted the plastid RNA primer removal processes in vitro. We also determined the crystal structure of the PEN1–dsDNA binary complex and explained the structural mechanism of the 5′ to 3′ exonuclease activity. Mutation of Pen1 resulted in the accumulation of ptDNA breaks, thereby compromising plastid function. These studies fill a critical gap that has long existed in the understanding of ptDNA replication. The enzyme involved in RNA primer removal during ptDNA replication has long remained mysterious. Researchers have now found that PEN1 is responsible for this process, thereby filling a critical gap in our understanding of ptDNA replication.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 7","pages":"1325-1338"},"PeriodicalIF":13.6,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144479080","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}
Nature PlantsPub Date : 2025-06-20DOI: 10.1038/s41477-025-02045-2
{"title":"Naming is caring","authors":"","doi":"10.1038/s41477-025-02045-2","DOIUrl":"10.1038/s41477-025-02045-2","url":null,"abstract":"We can now carry in our pockets applications that accurately identify the plants around us. These are interesting tools for researchers, but they also help everyone to appreciate the diversity of the natural world.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 6","pages":"1091-1092"},"PeriodicalIF":13.6,"publicationDate":"2025-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41477-025-02045-2.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144335092","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}
Nature PlantsPub Date : 2025-06-20DOI: 10.1038/s41477-025-02021-w
{"title":"Identification of transit peptides that boost plastid protein import in different tissues and plant species","authors":"","doi":"10.1038/s41477-025-02021-w","DOIUrl":"10.1038/s41477-025-02021-w","url":null,"abstract":"The efficient delivery of proteins into plastids is key to using plastid protein engineering in biotechnology applications, a fact that is often overlooked. This study identifies transit peptides that efficiently import different passenger proteins into major plastid types across plant species, offering an effective tool for manipulating plastid-related traits.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 7","pages":"1231-1232"},"PeriodicalIF":13.6,"publicationDate":"2025-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144328985","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}
{"title":"Regulation of m6A RNA reader protein OsECT3 activity by lysine acetylation in the cold stress response in rice","authors":"Nini Ma, Peizhe Song, Ziyang Liu, Yangjie Li, Zhihe Cai, Mengyue Ding, Xuan Ma, Qiutao Xu, Yaping Yue, Tangdi Luo, Dao-Xiu Zhou, Guifang Jia, Yu Zhao","doi":"10.1038/s41477-025-02013-w","DOIUrl":"10.1038/s41477-025-02013-w","url":null,"abstract":"N6-Methyladenosine (m6A) reader proteins, which recognize m6A to regulate RNA metabolism, are important for plant adaptation to the changing environment. It remains unknown how the activities of plant m6A reader proteins are regulated in plant responses to stress. Here we show that the rice m6A reader protein EVOLUTIONARILY CONSERVED C-TERMINAL REGION 3 (OsECT3), required for rice tolerance to cold, is post-translationally modified by lysine acetylation, which reduces its m6A-binding activity. Under cold conditions, OsECT3 acetylation is reduced by cold-induced histone deacetylase HDA705 and low ACLA2-sourced acetyl-CoA levels, resulting in an increase in OsECT3 m6A-binding activity, the accumulation of cold-response-related mRNAs and improved tolerance of rice to cold stress. These results unravel a regulatory mechanism of an m6A reader protein to dynamically control m6A RNA levels under stress and suggest a link between lysine acetylation, metabolism and m6A pathways. Ma et al. report a regulatory mechanism by which lysine acetylation of the m6A reader protein OsECT3 modulates its m6A-binding activity under cold stress. The reduced acetylation level stabilizes cold-responsive mRNAs to enhance cold tolerance in rice.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"11 6","pages":"1165-1180"},"PeriodicalIF":13.6,"publicationDate":"2025-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144335093","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}