Journal of Experimental Botany最新文献_第2页

Differential regulation of 26S proteasome activity, abundance, and transcription during leaf development and senescence. 叶片发育和衰老过程中26S蛋白酶体活性、丰度和转录的差异调控。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/eraf274

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":"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.","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}

引用次数: 0

Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization. 叶绿体中的蛋白质静止和蛋白质质量控制：与蛋白质错误定位相关的机制和新见解。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/eraf182

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":"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.","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}

引用次数: 0

Four guidelines to identify bona fide protease-substrate pairs. 鉴定真正蛋白酶底物对的四个准则。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/eraf194

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":"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.","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}

引用次数: 0

Acylamino acid-releasing enzyme, a bifunctional protease with a potential role in aging. 酰基氨基酸释放酶（AARE）是一种双功能蛋白酶，在衰老过程中具有潜在作用。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/eraf169

Sebastian N W Hoernstein, Alessandra A Miniera, Ralf Reski

{"title":"Acylamino acid-releasing enzyme, a bifunctional protease with a potential role in aging.","authors":"Sebastian N W Hoernstein, Alessandra A Miniera, Ralf Reski","doi":"10.1093/jxb/eraf169","DOIUrl":"10.1093/jxb/eraf169","url":null,"abstract":"Acylamino acid-releasing enzyme (AARE) is a highly evolutionary conserved, bifunctional serine protease. In its exopeptidase mode, AARE cleaves N-terminally acetylated or otherwise blocked amino acids from the N-terminus of peptides, and probably even intact proteins. In its endopeptidase mode, AARE cleaves oxidised proteins at internal positions. Although AARE function was discovered 50 years ago and has been biochemically characterized in various organisms, the precise role of this protease in cellular physiology remains elusive. Several other names for AARE do exist in literature, such as acylpeptide hydrolase, acylaminoacyl peptidase, and oxidised protein hydrolase. Recently, the first AARE null mutants have been described in the model moss Physcomitrium patens (Physcomitrella). Comparisons with T-DNA mutants in Arabidopsis thaliana revealed a role for AARE in the timing of the developmental transition from the vegetative to the reproductive state, as well as in the determination of life span. Loss of AARE function was accompanied by a striking increase in oxidised proteins, a hallmark of cellular aging. In mammals, AARE activity is linked to proteasomal function, and dysregulation of AARE function has been observed in different types of cancer and age-related pathologies. Here, we compile the current knowledge on molecular and biological functions of this protease, aiming to derive common roles of AARE in cellular physiology, and potentially in aging, but also highlight differences between species isoforms.","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4262-4278"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12485367/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144009903","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}

引用次数: 0

Balance of chlorophyll synthesis and thylakoid protein quality control influences chloroplast development in var2 mutants. 叶绿素合成平衡和类囊体蛋白质量控制影响var2叶绿体发育。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/eraf177

Peiyi Wang, Lin Zhu, Xiaomin Wang, Yanan Zhai, Jiahui Zhong, Hongchang Zhang, Jingxia Shao, Xiayan Liu, Fei Yu, Yafei Qi

{"title":"Balance of chlorophyll synthesis and thylakoid protein quality control influences chloroplast development in var2 mutants.","authors":"Peiyi Wang, Lin Zhu, Xiaomin Wang, Yanan Zhai, Jiahui Zhong, Hongchang Zhang, Jingxia Shao, Xiayan Liu, Fei Yu, Yafei Qi","doi":"10.1093/jxb/eraf177","DOIUrl":"10.1093/jxb/eraf177","url":null,"abstract":"Filamentous temperature-sensitive H (FtsH) is a major protease for thylakoid protein quality control in photosynthetic organisms. Mutations of the AtFtsH2 subunit in Arabidopsis result in yellow variegated2 (var2) mutants. Genetic screening of ENHANCER OF VARIEGATION (EVR) loci provides new insights into the role of FtsH in chloroplast development beyond the degradation of photodamaged D1 protein. Here, using Arabidopsis, we uncover a novel function of EVR3, previously reported as ETHYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN1 (EGY1), in regulating chlorophyll biosynthesis by association with the H subunit of magnesium chelatase (CHLH). Additionally, we identify a new var2 enhancer mutant, evr4-1, caused by a missense mutation in CHLH. The evr4-1 mutant shows a significant decline in accumulation of light-harvesting complexes rather than in photosystem II core proteins, while evr3 evr4 double mutants exhibit synthetic lethal phenotypes accompanied by a drastic reduction in the accumulation of chlorophyll and light-harvesting complexes. Furthermore, disruption of the thylakoid protein sorting pathway mediated by the chloroplast Signal Recognition Particle 54 kDa protein mitigates the chloroplast development defect in var2-4 evr4-1. Our findings underscore the critical role of thylakoid FtsH for thylakoid protein quality control when chlorophyll biosynthesis is disrupted.","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4359-4373"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143982671","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

ECLIPSE mediates selective degradation of inner nuclear membrane protein in plants. ECLIPSE介导植物核膜蛋白的选择性降解。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/eraf167

Enrico Calvanese, Min Jia, Olivia Xie, Yangnan Gu

{"title":"ECLIPSE mediates selective degradation of inner nuclear membrane protein in plants.","authors":"Enrico Calvanese, Min Jia, Olivia Xie, Yangnan Gu","doi":"10.1093/jxb/eraf167","DOIUrl":"10.1093/jxb/eraf167","url":null,"abstract":"The inner nuclear membrane (INM) hosts a unique set of membrane proteins essential for nuclear functions. Proteolytic removal of mislocalized or defective membrane proteins is of critical importance for maintaining the homeostasis and integrity of the INM. Previous studies revealed that INM protein degradation depends on a specialized ubiquitin-proteasome system termed INM-associated degradation (INMAD) in plants, requiring the CDC48 complex and the 26S proteasome for membrane protein retrotranslocation and destruction, respectively. However, details of the adaptor proteins that link membrane substrates to the CDC48/proteasome degradation machinery are still lacking in the pathway. Here, we report the discovery of ECLIPSE, a previously uncharacterized protein that may serve as such a molecular bridge in the degradation of the conserved INM protein SUN1. We demonstrate that ECLIPSE physically associates with CDC48 and exhibits strong transcriptional co-regulation with multiple established plant INMAD components. Mechanistically, ECLIPSE may act as an adaptor through its dual-domain architecture: its C-terminal PUB domain mediates direct interaction with CDC48, while its N-terminal ubiquitin-associated domain recognizes ubiquitinated INM substrates. Genetic and biochemical analyses further established that ECLIPSE is required for SUN1 protein degradation in Arabidopsis, supporting its role in the turnover of at least some INM proteins in plants.","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4326-4339"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12485365/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144021983","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}

引用次数: 0

The CAPE1 peptide confers resistance against bacterial wilt in tomato. CAPE1 肽能增强番茄对细菌性枯萎病的抗性。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/eraf145

Weiqi Zhang, Marc Planas-Marquès, Moyan Liang, Qingshan Zhang, Annemarie Vermeulen, Farnusch Kaschani, Markus Kaiser, Frank L W Takken, Nuria S Coll, Marc Valls

{"title":"The CAPE1 peptide confers resistance against bacterial wilt in tomato.","authors":"Weiqi Zhang, Marc Planas-Marquès, Moyan Liang, Qingshan Zhang, Annemarie Vermeulen, Farnusch Kaschani, Markus Kaiser, Frank L W Takken, Nuria S Coll, Marc Valls","doi":"10.1093/jxb/eraf145","DOIUrl":"10.1093/jxb/eraf145","url":null,"abstract":"Bacterial wilt caused by Ralstonia solanacearum is one of the most destructive bacterial diseases for which no effective treatment exists. There is an urgent need to understand the basis of resistance against this pathogen in order to engineer efficient strategies in the field. We previously demonstrated that resistant tomato plants limit bacterial movement in the apoplast and the xylem. As a first step to dissect the underlying mechanisms, we analysed the apoplast proteome upon challenge with R. solanacearum in the susceptible tomato cultivar Marmande and the resistant cultivar Hawaii 7996. Here, we described the xylem proteome in these same cultivars and compared it with the apoplastic proteome, revealing variety-dependent and infection-dependent changes. This proteomic analysis led to the identification of pathogenesis-related 1 (PR1) proteins as highly induced upon infection. Since PR1b was the most abundant PR1 protein in both the apoplast and the xylem, we concentrated on this family member to study the role of PR1s in the interaction between tomato and R. solanacearum. Surprisingly, lack of PR1b resulted in enhanced resistance to R. solanacearum in tomato, which could be due to an up-regulation of homologous genes in a compensatory effect as has been reported before. PR1 processing by an unknown protease in tomato results in the generation of the CAPE peptide. Treatment of tomato plants with the CAPE1 peptide resulted in restriction of R. solanacearum growth, via defence gene reprogramming. Future work in the lab will help determine which tomato secreted proteases cleave PR1s to generate CAPEs.","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4340-4358"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12485366/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143772700","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}

引用次数: 0

Hacking the immune system: plant immune protease engineering for crop protection. 破解免疫系统：作物保护用植物免疫蛋白酶工程。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/eraf137

Mariana Schuster, Alexander L Ciattoni, Renier A L van der Hoorn

引用次数: 0

Silenced cutters: mechanisms and effects of protease inhibition in plant-pathogen interactions. 沉默切割器：植物与病原体相互作用中蛋白酶抑制的机制和作用。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/eraf156

Catarina Paiva-Silva, João Proença Pereira, Frederico Marcolino, Andreia Figueiredo, Rita B Santos

{"title":"Silenced cutters: mechanisms and effects of protease inhibition in plant-pathogen interactions.","authors":"Catarina Paiva-Silva, João Proença Pereira, Frederico Marcolino, Andreia Figueiredo, Rita B Santos","doi":"10.1093/jxb/eraf156","DOIUrl":"10.1093/jxb/eraf156","url":null,"abstract":"Proteases are essential enzymes in plants that play multiple roles in immunity, including molecular recognition, programmed cell death, and the degradation of pathogen proteins. During plant-pathogen interactions, both organisms have evolved mechanisms to regulate protease activity. Plants produce specific inhibitors to prevent excessive or harmful proteolysis, while pathogens counteract these defences by deploying molecules that block proteases and weaken plant immunity. Despite significant progress in understanding protease function, many regulatory mechanisms remain unexplored. This review examines the roles of endoproteases in plant responses to biotic stress and the diverse strategies employed by both plants and pathogens to modulate their activity. We discuss known protease inhibition mechanisms and highlight emerging methodologies that offer new insights into protease regulation. Additionally, we explore biotechnological applications, including genetic engineering and chemical inhibitors, aimed at enhancing plant resistance to pathogens. By integrating current knowledge with innovative research tools, we can uncover novel protease regulatory pathways and develop new strategies to improve plant resilience. Understanding these mechanisms not only advances fundamental plant biology but also holds potential for sustainable agricultural practices in the face of evolving pathogen threats.","PeriodicalId":15820,"journal":{"name":"Journal of Experimental Botany","volume":" ","pages":"4248-4261"},"PeriodicalIF":5.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12485229/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143999374","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}

引用次数: 0

RD21-like proteases: key effector hubs in plant-pathogen interactions. rd21样蛋白酶：植物与病原体相互作用的关键效应中心。

IF 5.7 2区生物学

Journal of Experimental Botany Pub Date : 2025-10-01 DOI: 10.1093/jxb/erae496

Jie Huang, Renier A L van der Hoorn

引用次数: 0