Hong Wei, Heyuan Zhu, Wei Ying, Hilde Janssens, Miroslav Kvasnica, Johan M Winne, Yongxiang Gao, Jiří Friml, Qian Ma, Shutang Tan, Xin Liu, Eugenia Russinova, Linfeng Sun
{"title":"Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1.","authors":"Hong Wei, Heyuan Zhu, Wei Ying, Hilde Janssens, Miroslav Kvasnica, Johan M Winne, Yongxiang Gao, Jiří Friml, Qian Ma, Shutang Tan, Xin Liu, Eugenia Russinova, Linfeng Sun","doi":"10.1016/j.xplc.2024.101181","DOIUrl":"https://doi.org/10.1016/j.xplc.2024.101181","url":null,"abstract":"<p><p>Brassinosteroids (BRs) are steroidal phytohormones indispensable for plant growth, development, and responses to environmental stresses. The export of bioactive BRs to the apoplast is essential for BR signalling initiation, which requires binding of BR molecule to the extracellular domains of the plasma membrane-localized receptor complex. We have previously shown that the Arabidopsis thaliana ATP-binding cassette (ABC) transporter, ABCB19, functions as a BR exporter, and together with its close homologue, ABCB1, positively regulate BR signalling. Here, we demonstrate that ABCB1 is another BR transporter. The ATP hydrolysis activity of ABCB1 was stimulated by bioactive BRs, and its transport activity was confirmed in proteoliposomes and protoplasts. Structures of ABCB1 in substrate-unbound (apo), brassinolide (BL)-bound, and ATP plus BL-bound states were determined. In the BL-bound structure, BL was bound to the hydrophobic cavity formed by the transmembrane domain, and triggered local conformational changes. Together, our data provide additional insights into the ABC transporter-mediated BR export.</p>","PeriodicalId":52373,"journal":{"name":"Plant Communications","volume":null,"pages":null},"PeriodicalIF":9.4,"publicationDate":"2024-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142577349","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}
Alvaro Santiago Larran, Jingyu Ge, Guiomar Martín, Juan Carlos de la Concepción, Yasin Dagdas, Julia Irene Qüesta
{"title":"Nucleo-cytoplasmic distribution of SAP18 reveals its dual function in splicing regulation and heat stress response in Arabidopsis.","authors":"Alvaro Santiago Larran, Jingyu Ge, Guiomar Martín, Juan Carlos de la Concepción, Yasin Dagdas, Julia Irene Qüesta","doi":"10.1016/j.xplc.2024.101180","DOIUrl":"https://doi.org/10.1016/j.xplc.2024.101180","url":null,"abstract":"<p><p>The dynamic shuttling of proteins between the nucleus and cytoplasm orchestrates vital functions in eukaryotes. Here, we unveil multifaceted functions of Arabidopsis Sin3-associated protein 18 kDa (SAP18) in regulating development and heat stress tolerance. Proteomic analysis demonstrated that SAP18 is a core component of the nuclear Apoptosis- and Splicing-Associated Protein (ASAP) complex in Arabidopsis, contributing to the precise splicing of genes associated with leaf development. Genetic analysis further confirmed SAP18's critical role in different developmental processes as part of the ASAP complex, including leaf morphogenesis and flowering time. Interestingly, upon heat shock SAP18 translocates from the nucleus to cytoplasmic stress granules and processing bodies. The heat-sensitive phenotype of SAP18 loss-of-function mutant revealed its novel role in plant thermoprotection. Our findings significantly expand our understanding of SAP18 relevance for plant growth, linking nuclear splicing with cytoplasmic stress responses, and providing new perspectives for future exploration of plant thermotolerance mechanisms.</p>","PeriodicalId":52373,"journal":{"name":"Plant Communications","volume":null,"pages":null},"PeriodicalIF":9.4,"publicationDate":"2024-10-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142559423","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}
Lili Chen, Melvin Rodriguez-Heredia, Guy T Hanke, Alexander V Ruban
{"title":"Distinct features of PsbS essential for mediating plant photoprotection.","authors":"Lili Chen, Melvin Rodriguez-Heredia, Guy T Hanke, Alexander V Ruban","doi":"10.1016/j.xplc.2024.101179","DOIUrl":"https://doi.org/10.1016/j.xplc.2024.101179","url":null,"abstract":"<p><p>For optimum photosynthetic productivity it is crucial for plants to swiftly transition between light harvesting and photoprotective states as light conditions change in the field. The PsbS protein plays a pivotal role in this process by switching the light harvesting antenna, LHCII, into the photoprotective state, qE, to avoid photoinhibition in high light environment. However, the molecular mechanism of PsbS action upon LHCII have remained unclear. In our study, we identified its specific aminoacid domains that are essential for the function. Using the aminoacid point-mutagenesis of PsbS in vivo we found that the activation of photoprotection involves dynamic changes in the oligomeric state and conformation of PsbS, with two residues, E67 and E173, playing a key role in this process. Further, the replacement of hydrophobic phenylalanine residues in transmembrane helixes II (F83, F84, F87) and IV (F191, F193, F194) with tyrosine revealed that phenylalanine localised in helix IV could play a significant role in hydrophobic interactions of PsbS with LHCII. The removal of the 3<sub>10</sub> helix (H3) aminoacids I74, Y75, E76 did not affect the amplitude but resulted in a strongly delayed recovery of qE in darkness. These findings provide new insights into the molecular architecture of PsbS that are essential for regulating light harvesting in higher plants. Moreover, the combination of experimental mutagenesis with AI-assisted protein folding evolutionary scale model approach (ESMFold) opens new avenues for intelligently manipulating protein functions in silico to streamline and evaluate the experimental point mutagenesis strategies.</p>","PeriodicalId":52373,"journal":{"name":"Plant Communications","volume":null,"pages":null},"PeriodicalIF":9.4,"publicationDate":"2024-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142548885","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":"Natural variation in OsMADS1 transcript splicing affects rice grain thickness and quality through influencing monosaccharide loading to endosperm.","authors":"Rongjia Liu, Da Zhao, Pingbo Li, Duo Xia, Qingfei Feng, Lu Wang, Yipei Wang, Huan Shi, Yin Zhou, Fangying Chen, Guangming Lou, Hanyuan Yang, Haozhou Gao, Bian Wu, Junxiao Chen, Guanjun Gao, Qinglu Zhang, Jinghua Xiao, Xianghua Li, Lizhong Xiong, Yibo Li, Zichao Li, Aiqing You, Yuqing He","doi":"10.1016/j.xplc.2024.101178","DOIUrl":"https://doi.org/10.1016/j.xplc.2024.101178","url":null,"abstract":"<p><p>Grain size is a critical determinant of both grain weight and quality in rice, encompassing grain length, width and thickness. Despite the extensive regulatory networks for determining grain length and width, elucidation of a pathway for grain thickness remains elusive. Here, we present the map-based cloning and characterization of qGT3, a major quantitative trait locus for grain thickness in rice, which encodes MADS-domain transcription factor OsMADS1. Our findings demonstrated that OsMADS1 regulates grain thickness by affecting sugar delivery during grain filling. We further showed that OsMADS1 modulates the expression of downstream monosaccharide transporter gene MST4. Notably, a natural variation leads to alternative splicing and thus a truncated OsMADS1 protein with attenuated transcriptional repressor activity. The truncated OsMADS1 protein results in increased expression of MST4, leading to enhanced loading of monosaccharides into developing endosperm, thereby augmenting grain thickness, and improving grain quality. Additionally, our results revealed that NF-YB1 and NF-YC12 interact directly with OsMADS1, acting as cofactors to enhance its transcriptional activity towards MST4. Collectively, these findings reveal a novel molecular mechanism underlying grain thickness regulation that is controlled by the OsMADS1-NF-YB1-YC12 complex, which has great potential for synergistic improvement of grain yield and quality in rice.</p>","PeriodicalId":52373,"journal":{"name":"Plant Communications","volume":null,"pages":null},"PeriodicalIF":9.4,"publicationDate":"2024-10-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142570067","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}
Yang Han, Jianxiang Wu, Qian-Hao Zhu, Chu-Yu Ye, Xinxin Li
{"title":"Assembling a reference-quality genome and resequencing diverse accessions of Beckmannia syzigachne provide insights into population structure and gene family evolution.","authors":"Yang Han, Jianxiang Wu, Qian-Hao Zhu, Chu-Yu Ye, Xinxin Li","doi":"10.1016/j.xplc.2024.101174","DOIUrl":"https://doi.org/10.1016/j.xplc.2024.101174","url":null,"abstract":"","PeriodicalId":52373,"journal":{"name":"Plant Communications","volume":null,"pages":null},"PeriodicalIF":9.4,"publicationDate":"2024-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142480443","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}