Search results for: TOM1like
#38874374 
2024/06/14
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Modulation of abscisic acid signaling via endosomal TOL proteins.
The phytohormone abscisic acid (ABA) functions in the control of plant stress responses, particularly in drought stress. A significant mechanism in attenuating and terminating ABA signals involves regulated protein turnover, with certain ABA receptors, despite their main presence in the cytosol and nucleus, subjected to vacuolar degradation via the Endosomal Sorting Complex Required for Transport (ESCRT) machinery. Collectively our findings show that discrete TOM1-LIKE (TOL) proteins, which are functional ESCRT-0 complex substitutes in plants, affect the trafficking for degradation of core components of the ABA signaling and transport machinery. TOL2,3,5 and 6 modulate ABA signaling where they function additively in degradation of ubiquitinated ABA receptors and transporters. TOLs colocalize with their cargo in different endocytic compartments in the root epidermis and in guard cells of stomata, where they potentially function in ABA-controlled stomatal aperture. Although the tol2/3/5/6 quadruple mutant plant line is significantly more drought-tolerant and has a higher ABA sensitivity than control plant lines, it has no obvious growth or development phenotype under standard conditions, making the TOL genes ideal candidates for engineering to improved plant performance.Jeanette Moulinier-Anzola, Maximilian Schwihla, Rebecca Lugsteiner, Nils Leibrock, Mugurel I Feraru, Irma Tkachenko, Christian Luschnig, Elsa Arcalis, Elena Feraru, Jorge Lozano-Juste, Barbara Korbei
1309 related Products with: Modulation of abscisic acid signaling via endosomal TOL proteins.
1mg100 mg1010 mg501 mg2 1 G 1KG1 mL10
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#35932761 2022/08/05
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Broad-spectrum chemicals block ROS detoxification to prevent plant fungal invasion.
Plant diseases cause a huge impact on food security and are of global concern. While application of agrochemicals is a common approach in the control of plant diseases currently, growing drug resistance and the impact of off-target effects of these compounds pose major challenges. The identification of pathogenicity-related virulence mechanisms and development of new chemicals that target these processes are urgently needed. One such virulence mechanism is the detoxification of reactive oxygen species (ROS) generated by host plants upon attack by pathogens. The machinery of ROS detoxification might therefore serve as a drug target for preventing plant diseases, but few anti-ROS-scavenging drugs have been developed. Here, we show that in the model system Botrytis cinerea secretion of the cytochrome c-peroxidase, BcCcp1 removes plant-produced HO and promotes pathogen invasion. The peroxidase secretion is modulated by a Tom1-like protein, BcTol1, through physical interaction. We show that BcTol1 is regulated at different levels to enhance the secretion of BcCcp1 during the early infection stage. Inactivation of either BcTol1 or BcCcp1 leads to dramatically reduced virulence of B. cinerea. We identify two BcTol1-targeting small molecules that not only prevent B. cinerea invasion but also have effective activity against a wide range of plant fungal pathogens without detectable effect on the hosts. These findings reveal a conserved mechanism of ROS detoxification in fungi and provide a class of potential fungicides to control diverse plant diseases. The approach described here has wide implications for further drug discovery in related fields.Qianqian Yang, Jinguang Yang, Yameng Wang, Juan Du, Jianan Zhang, Ben F Luisi, Wenxing Liang
2628 related Products with: Broad-spectrum chemicals block ROS detoxification to prevent plant fungal invasion.
50 50 ug50 ug50 ug50 ug50.00 ug1 mg.25 mg1 module50 ug
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#34828351 2021/10/29
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Comparative RNA-Seq Analysis Reveals Potentially Resistance-Related Genes in Response to Bacterial Canker of Tomato.
Tomato is one of the most important crops for human consumption. Its production is affected by the actinomycete subsp. (), one of the most devastating bacterial pathogens of this crop. Several wild tomato species represent a source of natural resistance to . Here, we contrasted the transcriptomes of the resistant wild tomato species LA2157 and the susceptible species cv. Ailsa Craig, during the first 24 h of challenge with . We used three analyses approaches which demonstrated to be complementary: mapping to reference genome SL3.0; semi de novo transcriptome assembly; and de novo transcriptome assembly. In a global context, transcriptional changes seem to be similar between both species, although there are some specific genes only upregulated in during interaction, suggesting that the resistance regulatory mechanism probably diverged during the domestication process. Although showed enriched functional groups related to defense, displayed a higher number of induced genes related to bacterial, oomycete, and fungal defense at the first few hours of interaction. This study revealed genes that may contribute to the resistance phenotype in the wild tomato species, such as those that encode for a polyphenol oxidase E, diacyl glycerol kinase, TOM1-like protein 6, and an ankyrin repeat-containing protein, among others. This work will contribute to a better understanding of the defense mechanism against , and the development of new control methods.Leonardo I Pereyra-Bistraín, Cesaré Ovando-Vázquez, Alejandra Rougon-Cardoso, Ángel G Alpuche-Solís
1384 related Products with: Comparative RNA-Seq Analysis Reveals Potentially Resistance-Related Genes in Response to Bacterial Canker of Tomato.
100 UG1 module1 module1 module1 module1 module1 module96 wells (1 kit)1 module1 module
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#32087370 2020/02/19
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TOLs Function as Ubiquitin Receptors in the Early Steps of the ESCRT Pathway in Higher Plants.
Protein abundance and localization at the plasma membrane (PM) shapes plant development and mediates adaptation to changing environmental conditions. It is regulated by ubiquitination, a post-translational modification crucial for the proper sorting of endocytosed PM proteins to the vacuole for subsequent degradation. To understand the significance and the variety of roles played by this reversible modification, the function of ubiquitin receptors, which translate the ubiquitin signature into a cellular response, needs to be elucidated. In this study, we show that TOL (TOM1-like) proteins function in plants as multivalent ubiquitin receptors, governing ubiquitinated cargo delivery to the vacuole via the conserved Endosomal Sorting Complex Required for Transport (ESCRT) pathway. TOL2 and TOL6 interact with components of the ESCRT machinery and bind to K63-linked ubiquitin via two tandemly arranged conserved ubiquitin-binding domains. Mutation of these domains results not only in a loss of ubiquitin binding but also altered localization, abolishing TOL6 ubiquitin receptor activity. Function and localization of TOL6 is itself regulated by ubiquitination, whereby TOL6 ubiquitination potentially modulates degradation of PM-localized cargoes, assisting in the fine-tuning of the delicate interplay between protein recycling and downregulation. Taken together, our findings demonstrate the function and regulation of a ubiquitin receptor that mediates vacuolar degradation of PM proteins in higher plants.Jeanette Moulinier-Anzola, Maximilian Schwihla, Lucinda De-Araújo, Christina Artner, Lisa Jörg, Nataliia Konstantinova, Christian Luschnig, Barbara Korbei
1121 related Products with: TOLs Function as Ubiquitin Receptors in the Early Steps of the ESCRT Pathway in Higher Plants.
148 assays 2 Pieces/Box24 tests
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#24699223 2014/04/03
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Expression of Arabidopsis TOL genes.
A strict control of abundance and localization of plasma membrane proteins is essential for plants to be able to respond quickly and accurately to a changing environment. The proteins responsible for the initial recognition and concentration of ubiquitinated plasma membrane proteins destined for degradation, are well characterized in mammals and yeast, (1) yet no clear orthologs were found in plants. (2) Recently, we have identified a family of proteins in higher plants, which function in vacuolar targeting and subsequent degradation of ubiquitinated plasma membrane proteins (3,4) termed TOM1-like (TOL) proteins.Jeanette Moulinier-Anzola, Lucinda De-Araujo, Barbara Korbei
2968 related Products with: Expression of Arabidopsis TOL genes.
1KG 100 G100 5 μg 100 G 500 G
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#24316203 2013/12/05
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Arabidopsis TOL proteins act as gatekeepers for vacuolar sorting of PIN2 plasma membrane protein.
Controlling variations in plasma membrane (PM) protein abundance is of utmost importance for development in higher plants. For modulating PM protein activity, endocytosed proteins can be either cycled between PM and endosomes or sorted for their irreversible inactivation to lysosomes/vacuoles. Cargo ubiquitination triggers vacuolar delivery for degradation, which is controlled by Endosomal Sorting Complex Required for Transport (ESCRT). Essential parts of this machinery are conserved across kingdoms, but determinants liable for initial recognition and concentration of ubiquitinated cargo have not been identified in plants. Here, we describe members of an Arabidopsis TOL (TOM1-LIKE) family as ubiquitin binding proteins that act redundantly in control of plant morphogenesis. Specifically, tol mutant combinations exhibit defects that reflect alterations in responses mediated by the phytohormone auxin. Consistently, we provide evidence for a role of TOLs in recognition and further endocytic sorting of a PIN-FORMED (PIN)-type auxin carrier protein at the PM, modulating dynamic auxin distribution and associated growth responses. Such TOL-dependent vacuolar sorting depends on cargo ubiquitination and coincides with dynamic rearrangements in TOL distribution. Collectively, these findings lead us to suggest a function for TOLs early in the passage of endocytosed ubiquitinated PM cargo, acting as gatekeepers for degradative protein sorting to the vacuole.Barbara Korbei, Jeanette Moulinier-Anzola, Lucinda De-Araujo, Doris Lucyshyn, Katarzyna Retzer, Muhammad A Khan, Christian Luschnig
1763 related Products with: Arabidopsis TOL proteins act as gatekeepers for vacuolar sorting of PIN2 plasma membrane protein.
100μg50 assays0.1 ml50 assays0.5mg1x96 well plate100μg0.05 mg0.1mg100 assays
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#16847136 //
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Involvement of THH1, an Arabidopsis thaliana homologue of the TOM1 gene, in tobamovirus multiplication.
The TOM1 and TOM3 genes of Arabidopsis thaliana encode homologous proteins that are required for tobamovirus multiplication. Although the A. thaliana genome encodes another TOM1-like gene, THH1, the tobamovirus coat protein (CP) does not accumulate to a detectable level in the tom1 tom3 double mutant. Here, double and triple mutants of tom1, tom3 and thh1 were generated to investigate whether THH1 functions to support tobamovirus multiplication. In the tom1 thh1 double mutant, the tobamovirus CP accumulated to a level that was detectable, but lower than that in the tom1 single mutant. In tom1 tom3 double-mutant lines overexpressing THH1, the tobamovirus CP accumulated to a level similar to that observed in wild-type plants. These results suggest that THH1 supports tobamovirus multiplication, but to a lesser extent than TOM1 and TOM3. The expression level of THH1 is lower than that of TOM1 and TOM3, which might explain the smaller contribution of THH1 to tobamovirus multiplication.Koki Fujisaki, Gerald B Ravelo, Satoshi Naito, Masayuki Ishikawa
2864 related Products with: Involvement of THH1, an Arabidopsis thaliana homologue of the TOM1 gene, in tobamovirus multiplication.
100 μg100 μg2 Pieces/Box100 μg100 μg
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#14613930 2003/11/12
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Endofin recruits TOM1 to endosomes.
Endofin is an endosomal protein implicated in regulating membrane trafficking. It is characterized by the presence of a phosphatidylinositol 3-phosphate-binding FYVE domain positioned in the middle of the molecule. To determine its potential effectors or binding partners, we used the carboxyl-terminal half of endofin as bait to screen a human brain cDNA library in a yeast two-hybrid system. Three clones that encode TOM1 were recovered. TOM1 is a protein closely related to the VHS (VPS-27, Hrs, and STAM) domain-containing GGA family. Although the function of the GGAs in mediating Golgi to lysosomal trafficking is well established, the subcellular localization and function of TOM1 remain unknown. Glutathione S-transferase pull-down assays as well as co-immunoprecipitation experiments confirmed that the carboxyl-terminal half of endofin binds specifically to the carboxyl-terminal region of TOM1. Neither SARA nor Hrs, two other FYVE domain proteins, interact with this region of TOM1. Moreover, endofin does not interact with the analogous region of two other members of the TOM1 protein family, namely, TOM1-like 1 (TOM1-L1) or TOM1-like 2 (TOM1-L2). The carboxyl-terminal region of TOM1 was used as immunogen to generate TOM1-specific antibody. This antibody can distinguish TOM1 from the other family members as well as coimmunoprecipitate endogenous endofin. It also revealed the primarily cytosolic distribution of TOM1 in a variety of cell types by immunofluorescence analyses. In addition, sucrose density gradient analysis showed that both TOM1 and endofin can be detected in cellular compartments marked by the early endosomal marker EEA1. A marked recruitment of TOM1 to endosomes was observed in cells overexpressing endofin or its carboxyl-terminal fragment, indicating TOM1 to be an effector for endofin and suggesting a possible role for TOM1 in endosomal trafficking.Li-Fong Seet, Ningsheng Liu, Brendon J Hanson, Wanjin Hong
2090 related Products with: Endofin recruits TOM1 to endosomes.
100ul100 μg100 μg 100ul1 module1 mL96 50G430 tests1 mL1 module
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#11836427 //
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Complete inhibition of tobamovirus multiplication by simultaneous mutations in two homologous host genes.
The TOM1 gene of Arabidopsis thaliana encodes a putative multipass transmembrane protein which is necessary for the efficient multiplication of tobamoviruses. We have previously shown that mutations severely destructive to the TOM1 gene reduce tobamovirus multiplication to low levels but do not impair it completely. In this report, we subjected one of the tom1 mutants (tom1-1) to another round of mutagenesis and isolated a new mutant which did not permit a detectable level of tobamovirus multiplication. In addition to tom1-1, this mutant carried a mutation referred to as tom3-1. Positional cloning showed that TOM3 was one of two TOM1-like genes in Arabidopsis. Based on the similarity between the amino acid sequences of TOM1 and TOM3, together with the results of a Sos recruitment assay suggesting that both TOM1 and TOM3 bind tobamovirus-encoded replication proteins, we propose that TOM1 and TOM3 play parallel and essential roles in the replication of tobamoviruses.Takuya Yamanaka, Takahiro Imai, Rena Satoh, Arata Kawashima, Miki Takahashi, Kayo Tomita, Kenji Kubota, Tetsuo Meshi, Satoshi Naito, Masayuki Ishikawa
2578 related Products with: Complete inhibition of tobamovirus multiplication by simultaneous mutations in two homologous host genes.
0.1ml (1mg/ml)100 ul0.1ml50ul96 assays 48 assays0.1ml0.1ml200ul100ug0.1ml (1mg/ml)48 assays
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#10329004 //
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TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1 and encode proteins similar to the endosomal proteins HGS and STAM.
The avian tom1 (target of myb 1) gene has been previously characterized from v-myb-transformed cells. We report here cloning of the human and mouse tom1 orthologs. Both genes are expressed ubiquitously, with the highest levels in skeletal muscle, brain, and intestines, as assessed by Northern blot and mRNA in situ hybridization. The N-terminal domain of the TOM1 protein shares similarity with HGS (hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (signal-transducing adaptor molecule), which are associated with vesicular trafficking at the endosome. A putative coiled-coil domain was also detected in the central part of the TOM1 protein. This domain structure suggests that TOM1 is another member of a family of genes implicated in the trafficking regulation of growth-factor-receptor complexes that are destined for degradation in the lysosome. We also show that a human paralog of TOM1 (TOM1-like gene 1) exists. Furthermore, we provide a transcription map over a 190-kb contig of the TOM1 region. This map includes its distal neighbors HMOX1 and MCM5 and two proximal novel genes, one of which is a HMG-box-containing gene (HMG2L1), and the other of unknown function. Using a genomic PAC clone, we demonstrate that the mouse Tom1 and Hmox1 genes are part of an as yet undescribed syntenic group between mouse chromosome 8C1 and human chromosome 22q13.1.E Seroussi, D Kedra, M Kost-Alimova, A C Sandberg-Nordqvist, I Fransson, J F Jacobs, Y Fu, H Q Pan, B A Roe, S Imreh, J P Dumanski