{"title":"A conserved AINTEGUMENTA-REVOLUTA module is a candidate to regulate carpel development in Lychee.","authors":"Huimin Hu, Xurong Fan, Qiuping Wu, Yanyang Liang, Yaxuan Xiao, Chengjie Chen, Fengqi Wu, Jiakun Zheng, Rui Xia, Jing Xu, Yanwei Hao, Zaohai Zeng","doi":"10.1093/jxb/eraf438","DOIUrl":"https://doi.org/10.1093/jxb/eraf438","url":null,"abstract":"<p><p>The lychee industry is vital to agricultural economies, boosting farmer livelihoods and regional growth. However, instability of flowering causes yield fluctuations, severely limiting industry sustainability. Stable pistil development in female flowers is essential for yield improvement, yet its molecular regulation remains poorly understood. Although AP2 transcription factors regulate floral organ differentiation and pistil development, their functional role in woody perennials like lychee is uncharacterized. In this study, two AP2 genes (LITCHI007109 and LITCHI010784) were found to exhibit high and specific expression in carpels. LITCHI007109, designated as LcANT1, is an ortholog of Arabidopsis AINTEGUMENTA (ANT). We next systematically identified the direct downstream target genes of LcANT1, the set of which were significant enriched in biological processes related to floral organ development and carpel morphology. Notably, the carpel development-related gene LITCHI024703 (LcREV) exhibited a high level of co-expression with LcANT1. We found that the LcANT1 protein can directly bind to the promoter region of LcREV. Further evolutionary analysis indicates that the ANT-REV regulatory module is highly conserved in angiosperms, especially in Sapindaceae. Our findings establish a novel theoretical framework for understanding female flower development in lychee and offer critical gene resources and regulatory networks for molecular breeding strategies aimed at developing high-yield, stable cultivars.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145212789","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}
Pitter F Huesgen, Annick Stintzi, Andreas Schaller
{"title":"Plant proteases: guardians of proteome integrity and regulators of protein function.","authors":"Pitter F Huesgen, Annick Stintzi, Andreas Schaller","doi":"10.1093/jxb/eraf319","DOIUrl":"10.1093/jxb/eraf319","url":null,"abstract":"<p><p>Proteases degrade proteins that are damaged, misfolded, or no longer needed. This enables plants to repurpose their proteomes in response to environmental cues and adapt to adverse conditions. Proteases also play key roles in plant growth and development by the selective degradation of regulatory proteins. However, there is much more to proteases than just protein degradation. They can also act in a highly site-specific manner, ensuring protein maturation after subcellular targeting, regulating protein activity and function, and releasing or modulating peptide signals. Since their activity is irreversible and potentially deleterious, proteases are tightly controlled by endogenous inhibitors and other regulatory mechanisms. The reviews and research articles in this Special Issue put a timely spotlight on the fascinating diversity, function, and regulation of proteases in plants, discuss current challenges and technical developments, and provide a perspective on their use for crop protection.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4203-4206"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12485363/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144753453","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Terminomics for plant protease substrate discovery: successes, challenges, and new approaches.","authors":"Melissa Mantz, Paula Dewes, Pitter F Huesgen","doi":"10.1093/jxb/eraf173","DOIUrl":"10.1093/jxb/eraf173","url":null,"abstract":"<p><p>Plants contain hundreds of proteases that are involved in the regulation of virtually all cellular processes. Some proteases act as molecular shredders, resulting in degradation of their substrates. Others act more like scissors, cutting substrate proteins in a limited manner at specific sites to alter their activity, location, and function. Such tailored proteoforms share their sequence with the precursor form and sometimes only differ by the new, proteolytically modified polypeptide termini. Identification of protein termini is mandatory for unambiguous identification, but challenging in standard MS-based proteomics. Over the last two decades, various methods for the enrichment of N- and C-terminal peptides have been developed to enable proteome-wide characterization. Here we briefly introduce major approaches to protein termini enrichment and review current applications for plant protease substrate identification and profiling of proteolytic cleavage events in vivo. We highlight both successes and limitations, and discuss current improvements in sample preparation, data acquisition, MS instrumentation, and data analysis that promise to increase sensitivity, robustness, and ultimately utility of termini-centric proteomics.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4279-4293"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143985457","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}
{"title":"The biological functions of FtsH in plant organelle protein homeostasis.","authors":"Fei Wang, Yafei Qi, Fei Yu","doi":"10.1093/jxb/eraf135","DOIUrl":"10.1093/jxb/eraf135","url":null,"abstract":"<p><p>Both mitochondria and chloroplasts are capable of driving the electron transport chain reactions for ATP production that are essential for plant growth, development, and stress resilience. The maintenance of organelle protein homeostasis relies on the coordinated assembly of membrane protein complexes and the degradation of unassembled or damaged subunits. FtsH proteins, containing an ATPase domain and a protease domain, are a highly conserved ATP-dependent protease family in photosynthetic organisms. In plants, different FtsH family members are targeted to specific organelle membranes to orchestrate protein homeostasis. This review provides an updated overview of the functions of plant FtsHs in mitochondrial and chloroplastic protein homeostasis, focusing on their protease activity, chaperone-like functions, and substrate processing capabilities. Additionally, it highlights the regulatory mechanisms currently known to modulate the activity and stability of FtsH. Furthermore, we summarize the genetic modifier loci of AtFtsH2/VAR2 encoding the AtFtsH2 subunit of the thylakoid FtsH complex in Arabidopsis and also propose a potential role for the thylakoid FtsH in the degradation of unassembled photosynthetic proteins, particularly under conditions in which the chlorophyll biosynthetic pathway is disrupted.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4220-4231"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143764185","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}
{"title":"Host-dependent roles of hyphosphere keystone Massilia in organic phosphorus mineralization and AM fungal growth.","authors":"Ningkang Sun, Letian Wang, Gu Feng","doi":"10.1093/jxb/eraf339","DOIUrl":"https://doi.org/10.1093/jxb/eraf339","url":null,"abstract":"<p><p>The plant-arbuscular mycorrhizal (AM) fungi-hyphosphere bacteria forms a cross-kingdom holobiont driven by top-down carbon flow and bottom-up phosphorus (P) fluxes. Hyphosphere keystone bacteria, such as Massilia, can compensate for the limited capacity of AM fungi to mobilize organic phosphorus (Po), thereby enhancing fungal development and plant performance. However, how Massilia modulates its functional role across plant-fungal combinations remains unclear. To address this, we employed three plant-AM fungi pairings (medicago, maize, and sorghum) combined with either single Massilia inoculation or a defined synthetic hyphosphere bacterial community (SynCom). Across all combinations, Massilia significantly enhanced shoot biomass, plant P content, phosphatase activity, and Po mineralization. Interestingly, its effects were amplified by SynCom co-inoculation in maize and sorghum, while in medicago hyphosphere, Massilia alone was more effective. Community profiling revealed host-specific Massilia-mediated recruitment of bacteria with high phosphatase activity and indole-3-acetic acid production. Our findings demonstrate that, as a hyphosphere keystone taxon, Massilia adopts host-dependent functional strategies-promoting AM fungal growth and Po mineralization in medicago through phosphatase production, while relying on the growth-stimulation of beneficial bacteria to mediate similar effects in maize and sorghum.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145199622","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}
Gabriel Ferreras-Garrucho, Tania Chancellor, Uta Paszkowski
{"title":"Integrating single-cell omic techniques to resolve the spatio-temporal complexity of arbuscular mycorrhizal symbiosis.","authors":"Gabriel Ferreras-Garrucho, Tania Chancellor, Uta Paszkowski","doi":"10.1093/jxb/eraf404","DOIUrl":"https://doi.org/10.1093/jxb/eraf404","url":null,"abstract":"<p><p>Arbuscular mycorrhizal symbiosis (AMS) is a ubiquitous and ancient interaction between plant root systems and fungi of the Glomeromycotina subphylum. The resulting relationship is mutually beneficial and deeply intimate where the fungus intracellularly colonises root cortex cells to receive organic carbon and deliver minerals and water to the plant. Fungal colonisation of plant roots and cells is extremely dynamic and asynchronous across the root system. Symbiosis development must therefore result from spatio-temporally fine-tuned molecular control mechanisms of plant and fungus. Although the plant genetic program underpinning AMS has been extensively studied, little is known about its dynamic regulation across root cell layers and developmental stages of the association. Thus, many questions remain outstanding: how do different cell-types transcriptionally respond to AMS, how are distinct cell-type specific regulatory states coordinated, and what are the transcriptional activities in the fungus associated with discrete stages of root colonisation? The advent of single cell-based techniques now enables the high-resolution analysis to address these questions. In this review, we recapitulate the current knowledge on the spatio-temporal control of AMS, we evaluate the relevance of existing spatial datasets to AMS research and provide new perspectives for future study.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145199633","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}
{"title":"The multifaceted roles of plant aspartic proteases.","authors":"Xiaobo Yu, Tingting Feng","doi":"10.1093/jxb/eraf147","DOIUrl":"10.1093/jxb/eraf147","url":null,"abstract":"<p><p>Aspartic proteases are extensively distributed across plant species and are integral to various developmental and defense mechanisms. This review initially examines the classification, biochemical properties, and advancements in the understanding of the subcellular localization of plant aspartic proteases. Subsequently, it delves into the diverse functions of aspartic proteases in plant vegetative and reproductive development, as well as their roles in responding to abiotic and biotic stresses. Additionally, the review addresses the specific functions of aspartic proteases in particular plant species, such as carnivorous plants and leguminous plants involved in nitrogen fixation. Collectively, this synthesis provides a comprehensive overview of the current knowledge regarding the roles of aspartic proteases in plants.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4232-4247"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143780190","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}
Haojie Wang, Joost T van Dongen, Jos H M Schippers
{"title":"Differential regulation of 26S proteasome activity, abundance, and transcription during leaf development and senescence.","authors":"Haojie Wang, Joost T van Dongen, Jos H M Schippers","doi":"10.1093/jxb/eraf274","DOIUrl":"10.1093/jxb/eraf274","url":null,"abstract":"<p><p>Protein homeostasis controlled by the 26S proteasome plays a pivotal role in the adaption of plants to environmental stress, contributing to survival and longevity. During ageing in animals, proteasome activity declines, resulting in senescence; however, in plants, this is so far largely unexplored. In both Arabidopsis and barley, we found that genes encoding proteasomal subunits are up-regulated at the transcript level during the onset of leaf senescence. In contrast, at the protein level, a decrease in proteasomal subunit abundance was observed. Moreover, in Arabidopsis, 26S proteasome capacity deteriorates with leaf age, while 20S proteasome activity increases. In contrast, in barley, a potential increase in proteasome activity was observed with age. As ribosome-associated RNA levels of proteasomal subunits increase in Arabidopsis during senescence, it suggests a high turnover. Furthermore, chemical inhibition of the proteasome results in accelerated leaf senescence in Arabidopsis and barley. In Arabidopsis, 26S proteasome activity could be restored by external cytokinin application, resulting in delayed senescence. Finally, we identified several senescence-associated transcription factors that acts as novel transcriptional regulators of proteasomal genes in Arabidopsis. Taken together, this work provides new insights into the dynamic regulation of proteasome activity which deepens our understanding on leaf senescence in plants.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4374-4387"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144484668","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}
Nicolaj Jeran, Maxime Mercier, Paolo Pesaresi, Luca Tadini
{"title":"Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.","authors":"Nicolaj Jeran, Maxime Mercier, Paolo Pesaresi, Luca Tadini","doi":"10.1093/jxb/eraf182","DOIUrl":"10.1093/jxb/eraf182","url":null,"abstract":"<p><p>The dynamic rearrangement of the proteome and the maintenance of protein homeostasis (proteostasis) are crucial for the proper development and functionality of cellular compartments. Disruptions in proteostasis can severely compromise cellular health, leading to the accumulation of misfolded or mislocalized proteins prone to forming toxic aggregates. In chloroplasts, proteostasis presents unique challenges due to their endosymbiotic origin, complex subcompartmentalization, and constant exposure to reactive oxygen species (ROS) generated during photosynthesis. To counteract these challenges, chloroplasts employ sophisticated quality control systems, including chaperones, proteases, and protein degradation pathways such as ubiquitination and autophagy-related mechanisms. Additionally, cytosolic systems play a crucial role in regulating nuclear-encoded, plastid-targeted proteins, ensuring their proper delivery or degradation when defective. Within chloroplasts, specialized proteases, chaperones, and the chloroplast unfolded protein response (cpUPR) oversee protein quality and resolve aggregates to maintain functional integrity. This review critically examines mechanisms governing intracellular trafficking of plastid-targeted proteins, emphasizing key pathways and regulatory bottlenecks that, when disrupted, lead to the accumulation of mislocalized or orphan proteins. Particular focus is given to the signalling pathways that coordinate cytosolic and plastid effectors to sustain chloroplast function. Furthermore, we propose a novel role for PSBO, a subunit of the oxygen evolving complex associated with PSII, in linking proplastid-to-chloroplast differentiation with plastid quality control.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4294-4312"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12485368/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144019098","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Shuning Qi, Shamik Mazumdar, Yong Zou, Qun Yang, Simon Stael, Maxence James
{"title":"Four guidelines to identify bona fide protease-substrate pairs.","authors":"Shuning Qi, Shamik Mazumdar, Yong Zou, Qun Yang, Simon Stael, Maxence James","doi":"10.1093/jxb/eraf194","DOIUrl":"10.1093/jxb/eraf194","url":null,"abstract":"<p><p>Plant proteases are an important class of enzymes, with proposed involvement in various aspects of the plant life cycle. However, pinpointing authentic protease-substrate interactions remains challenging, which hinders a comprehensive understanding of the biological function of proteases. Moreover, a structured set of guidelines to validate protease substrates is lacking. In this review, we outline a minimum of four key guidelines that, when followed, can confirm the specificity of protease-substrate interaction for proteases that perform limited proteolysis and with specific cleavage sites: (i) the observation of substrate cleavage; (ii) the reduction in substrate cleavage due to protease inhibitors or (iii) genetic mutation of the protease; and (iv) a final proof of the specificity of the substrate cleavage site. It is important to emphasize that these guidelines are not universally applicable to all proteases. By creating a set of guidelines, summarizing current findings and proposing future research directions, this review aims to highlight innovative techniques that will improve the specificity and accuracy of protease research and facilitate a deeper understanding of the role of proteases in plant biology.</p>","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4313-4325"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12485226/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143998643","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}