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Structural and functional interrelationships of histone H2A with its variants H2A.Z and H2A.W in Arabidopsis 组蛋白H2A及其变体H2A的结构和功能相互关系。Z和H2A。W在拟南芥中
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-12 DOI: 10.1016/j.str.2025.04.015
Youchao Wang, Jiabing Wu, Shuoming Yang, Xiang Li, Jiachen Wang, Qinghe Lv, Xiaoyu Zhu, Guoliang Lu, Jinru Zhang, Wen-Hui Shen, Bing Liu, Jinzhong Lin, Aiwu Dong
{"title":"Structural and functional interrelationships of histone H2A with its variants H2A.Z and H2A.W in Arabidopsis","authors":"Youchao Wang, Jiabing Wu, Shuoming Yang, Xiang Li, Jiachen Wang, Qinghe Lv, Xiaoyu Zhu, Guoliang Lu, Jinru Zhang, Wen-Hui Shen, Bing Liu, Jinzhong Lin, Aiwu Dong","doi":"10.1016/j.str.2025.04.015","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.015","url":null,"abstract":"Multiple histone H2A variants are known in eukaryotes. However, the functional relationship between H2A and its variants in plants remains largely obscure. Using CRISPR-Cas9 editing, we generated a mutant lacking four H2A isoforms in Arabidopsis and analyzed the functional and structural relationships between H2A, H2A.Z, and H2A.W. RNA sequencing and phenotype analyses revealed mild changes in gene transcription and plant development in mutants lacking H2A, H2A.Z, or H2A.W compared with the wild-type plants. Chromatin immunoprecipitation sequencing analysis showed that H2A can substitute for both H2A.Z and H2A.W across the genome, including in euchromatin and heterochromatin regions. However, H2A.Z replaced both H2A and H2A.W primarily within the euchromatin regions. By using DNA and histones from Arabidopsis, we constructed nucleosomes containing H2A, H2A.Z, or H2A.W and resolved their cryogenic electron microscopy (cryo-EM) structures at near-atomic resolution. Collectively, the results reveal the structural similarity and functional redundancy of H2A and its variants in Arabidopsis.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"1 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143933507","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Structural insights into the human system y+L amino acid transporter complex 人体系统y+L氨基酸转运复合物的结构见解
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-09 DOI: 10.1016/j.str.2025.04.012
Lu Dai, Kangtai Xu, Ting Zhang, Xiaoting Wang, Qian Zeng, Hao Liang, Chenye Xu, Liuqing Yang, Zilong Wang, Renhong Yan
{"title":"Structural insights into the human system y+L amino acid transporter complex","authors":"Lu Dai, Kangtai Xu, Ting Zhang, Xiaoting Wang, Qian Zeng, Hao Liang, Chenye Xu, Liuqing Yang, Zilong Wang, Renhong Yan","doi":"10.1016/j.str.2025.04.012","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.012","url":null,"abstract":"System y<sup>+</sup>L facilitates the sodium-independent transport of cationic and sodium-dependent transport of neutral amino acids via heteromeric amino acid transporters. System y<sup>+</sup>L consists of either SLC7A6 (y<sup>+</sup>LAT2) or SLC7A7 (y<sup>+</sup>LAT1) and 4F2hc (SLC3A2). The y<sup>+</sup>LAT2-4F2hc complex mediates the exchange of <sub>L</sub>-lysine (Lys), <sub>L</sub>-arginine (Arg), <sub>L</sub>-leucine (Leu), and <sub>L</sub>-glutamine (Gln) and is important for the glutamate-glutamine cycle and ammonia clearance. c-Myc-driven upregulation of y<sup>+</sup>LAT2 in cancer enhances amino acid uptake and mTORC1 activation, promoting tumor growth. Its transport mechanism has remained unclear. Here, we determined the cryoelectron microscopic (cryo-EM) structures of the y<sup>+</sup>LAT2-4F2hc complex bound to either Arg or Leu at 3.60 Å and 3.58 Å resolution, respectively, revealing an outward-open conformation. Our structural analysis highlights conformational changes during transport, and functional assays validate critical residues involved in substrate binding and transport. These findings elucidate the molecular mechanism of the system y<sup>+</sup>L and provide a foundation for developing targeted therapies against y<sup>+</sup>LAT2.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"20 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143926679","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Sla2 is a core interaction hub for clathrin light chain and the Pan1/End3/Sla1 complex Sla2是网格蛋白轻链和Pan1/End3/Sla1复合物相互作用的核心枢纽
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-09 DOI: 10.1016/j.str.2025.04.013
George Draper-Barr, Lucas A. Defelipe, David Ruiz-Carrillo, Emil Gustavsson, Meytal Landau, Maria García-Alai
{"title":"Sla2 is a core interaction hub for clathrin light chain and the Pan1/End3/Sla1 complex","authors":"George Draper-Barr, Lucas A. Defelipe, David Ruiz-Carrillo, Emil Gustavsson, Meytal Landau, Maria García-Alai","doi":"10.1016/j.str.2025.04.013","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.013","url":null,"abstract":"The interaction network of Sla2, a vital endocytic mid-coat adaptor protein, undergoes constant rearrangement. Sla2 serves as a scaffold linking the membrane to the actin cytoskeleton, with its role modulated by the clathrin light chain (CLC), which inhibits Sla2’s function under certain conditions. We show that Sla2 has two independent binding sites for CLC: one previously described in homologs of fungi (Sla2) and metazoa (Hip1R), and a second found only in Fungi. We present the structural model of the Sla2 actin-binding domains in the context of regulatory structural domains by cryoelectron microscopy. We provide an interaction map of Sla2 and the regulatory proteins Sla1 and Pan1, predicted by AI modeling and confirmed by molecular biophysics techniques. Pan1 may compete with CLC for the conserved Sla2-binding site. These results enhance the mapping of crucial interactions at endocytic checkpoints and highlight the divergence between Metazoa and Fungi in this vital process.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"12 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143926907","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Structural basis of human uromodulin filament networks in uropathogen capture 人尿调蛋白丝网在尿路病原体捕获中的结构基础
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-08 DOI: 10.1016/j.str.2025.04.011
Andrew N. Chang, Gabriele Cerutti, Yuki Ogawa, Alia Basler, Willa Switzer, Mia Eng-Kohn, Carolyn Lee, Anthony W.P. Fitzpatrick
{"title":"Structural basis of human uromodulin filament networks in uropathogen capture","authors":"Andrew N. Chang, Gabriele Cerutti, Yuki Ogawa, Alia Basler, Willa Switzer, Mia Eng-Kohn, Carolyn Lee, Anthony W.P. Fitzpatrick","doi":"10.1016/j.str.2025.04.011","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.011","url":null,"abstract":"Uromodulin (UMOD), the most abundant protein in human urine, is essential for kidney function and urinary tract health. UMOD forms filaments that bind to uropathogenic bacteria, facilitating their aggregation and clearance from the urinary tract. Here, we present the cryo-electron microscopy (cryo-EM) structure of the bacteria-binding D10C domain of UMOD and reveal its binding to the filament core. The details of D10C-core binding explain the formation of distinct filament lattice architectures adopted by UMOD. The D10C-core binding interface gives rise to diverse filament lattice structures, ranging from open and expansive to compact and dense conformations, or a combination of both. We hypothesize that other molecules present in urine may act as cross-linking agents, further stabilizing this binding interface and facilitating the connection of individual filaments into larger networks capable of effectively trapping bacteria. Structural mapping of kidney disease-related mutations points toward the abolition of disulfide bonds and promotion of mutant UMOD aggregation.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"8 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143920768","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The YEATS domain is a selective reader of histone methacrylation YEATS结构域是组蛋白甲基化的选择性读卡器
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-07 DOI: 10.1016/j.str.2025.04.010
Dustin C. Becht, Jiabao Song, Karthik Selvam, Kejun Yin, Weizhi Bai, Yingming Zhao, Ronghu Wu, Y. George Zheng, Tatiana G. Kutateladze
{"title":"The YEATS domain is a selective reader of histone methacrylation","authors":"Dustin C. Becht, Jiabao Song, Karthik Selvam, Kejun Yin, Weizhi Bai, Yingming Zhao, Ronghu Wu, Y. George Zheng, Tatiana G. Kutateladze","doi":"10.1016/j.str.2025.04.010","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.010","url":null,"abstract":"Metabolically regulated lysine acylation modifications in proteins play a major role in epigenetic processes and cellular homeostasis. A new type of histone acylation, lysine methacrylation, has recently been identified but remains poorly characterized. Here, we show that lysine methacrylation can be generated through metabolism of sodium methacrylate and enzymatically removed in cells, and that the YEATS domain but not bromodomain recognizes this modification. Structural and biochemical analyses reveal the π-π-π-stacking mechanism for binding of the YEATS domain of ENL to methacrylated histone H3K18 (H3K18mc). Using mass spectrometry proteomics, we demonstrate that methacrylate induces global methacrylation of a set of proteins that differs from the set of methacrylated proteins associated with valine metabolism. These findings suggest that high levels of methacrylate may potentially perturb cellular functions of these proteins by altering protein methacrylation profiles.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"31 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143915676","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Asymmetric structure of podophage N4 from the Schitoviridae family reveals a type of tube-sheath short-tail architecture Schitoviridae家族的足噬体N4的不对称结构揭示了一种管鞘短尾结构
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-02 DOI: 10.1016/j.str.2025.04.008
Jing Zheng, Hao Pang, Hao Xiao, Junquan Zhou, Zhonghua Liu, Wenyuan Chen, Hongrong Liu
{"title":"Asymmetric structure of podophage N4 from the Schitoviridae family reveals a type of tube-sheath short-tail architecture","authors":"Jing Zheng, Hao Pang, Hao Xiao, Junquan Zhou, Zhonghua Liu, Wenyuan Chen, Hongrong Liu","doi":"10.1016/j.str.2025.04.008","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.008","url":null,"abstract":"The tails of the majority of reported podophages are typically composed of an adaptor, a nozzle, and a needle, and flanked by six or twelve fibers. However, the <em>Schitoviridae</em> family, as represented by podophage N4, exhibits a different tail architecture that remains poorly understood. In this study, we employed cryoelectron microscopy (cryo-EM) to determine the atomic structures of mature and empty podophage N4 particles. The N4 tail, which is connected to the head by a portal and flanked by 12 fibers, comprises an adaptor, a 12-fold extended tail tube encircled by a 6-fold tail sheath, and a plug. The extended tail sheath is composed of two proteins, gp65 and gp64. Furthermore, we identified two distinct tail conformations in the mature podophage N4. Our structures provide insights into the mechanisms of ejection and early transcription of podophage N4, as well as for N4-like phages and CrAssphages.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"2 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143897519","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Introducing Bonnie Murphy, Ville Kaila, Maxie Roessler, Volha Chukhutsina, Alisia Fadini, Sonya Hanson, Filipe Maia, and Kirill Kovalev 有请Bonnie Murphy， Ville Kaila, Maxie Roessler, Volha Chukhutsina, alicia Fadini, Sonya Hanson， Filipe Maia和Kirill Kovalev
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-01 DOI: 10.1016/j.str.2025.04.003
Bonnie J. Murphy, Ville R.I. Kaila, Maxie M. Roessler, Volha Chukhutsina, Alisia Fadini, Sonya M. Hanson, Filipe R.N.C. Maia, Kirill Kovalev
{"title":"Introducing Bonnie Murphy, Ville Kaila, Maxie Roessler, Volha Chukhutsina, Alisia Fadini, Sonya Hanson, Filipe Maia, and Kirill Kovalev","authors":"Bonnie J. Murphy, Ville R.I. Kaila, Maxie M. Roessler, Volha Chukhutsina, Alisia Fadini, Sonya M. Hanson, Filipe R.N.C. Maia, Kirill Kovalev","doi":"10.1016/j.str.2025.04.003","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.003","url":null,"abstract":"In this Voices article, we introduce eight impressive scientists at different career stages who spoke at the recent “8th Ringberg Workshop on Structural Biology (with FELs)” organized by Ilme Schlichting from the Max Planck Institute for Medical Research, Heidelberg. We asked the authors to tell us more about themselves and their exciting research.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"44 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143893085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Putting the brakes on endocytosis 抑制内吞作用
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-01 DOI: 10.1016/j.str.2025.04.001
Bernard T. Kelly
{"title":"Putting the brakes on endocytosis","authors":"Bernard T. Kelly","doi":"10.1016/j.str.2025.04.001","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.001","url":null,"abstract":"In this issue of <em>Structure</em>, Horatscheck et al.<span><span><sup>1</sup></span></span> report the isolation and characterization of two improved small molecule drugs for the selective inhibition of clathrin-mediated endocytosis.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"71 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143893155","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Cryo-ET unravels the mystery of Ad5-nCoV vaccines Cryo-ET揭开了Ad5-nCoV疫苗的神秘面纱
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-01 DOI: 10.1016/j.str.2025.04.006
Chang Liu, Zunlong Ke
{"title":"Cryo-ET unravels the mystery of Ad5-nCoV vaccines","authors":"Chang Liu, Zunlong Ke","doi":"10.1016/j.str.2025.04.006","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.006","url":null,"abstract":"The Ad5-nCoV vaccine (Convidecia) against COVID-19 showed promising clinical results. However, the molecular mechanisms underlying its high immunogenicity and potential adverse reactions have remained elusive. In this issue of <em>Structure</em>, Dong et al.<span><span><sup>1</sup></span></span> employed cryo-electron tomography as a powerful technique to show that abundant prefusion spike protein formation is induced by Ad5-nCoV vaccines.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"12 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143893156","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Functional conformations or poor mimetics? 功能构象还是拙劣的模仿者？
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-01 DOI: 10.1016/j.str.2025.04.002
Hugues Nury, Rouslan G. Efremov
{"title":"Functional conformations or poor mimetics?","authors":"Hugues Nury, Rouslan G. Efremov","doi":"10.1016/j.str.2025.04.002","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.002","url":null,"abstract":"Membrane proteins function within lipid membranes but require mimetics for structural studies. In this issue of <em>Structure</em>, Hoffmann et al.<span><span><sup>1</sup></span></span> show how different mimetics bias the conformational spectrum of the MsbA transporter. This study highlights the need for improved membrane mimetics and sustained efforts to link conformations to function.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"45 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143893157","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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