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1.
Plant Cell ; 34(8): 2892-2906, 2022 07 30.
Artículo en Inglés | MEDLINE | ID: mdl-35567527

RESUMEN

A key function of photoreceptor signaling is the coordinated regulation of a large number of genes to optimize plant growth and development. The basic helix loop helix (bHLH) transcription factor MYC2 is crucial for regulating gene expression in Arabidopsis thaliana during development in blue light. Here we demonstrate that blue light induces the SUMOylation of MYC2. Non-SUMOylatable MYC2 is less effective in suppressing blue light-mediated photomorphogenesis than wild-type (WT) MYC2. MYC2 interacts physically with the SUMO proteases SUMO PROTEASE RELATED TO FERTILITY1 (SPF1) and SPF2. Blue light exposure promotes the degradation of SPF1 and SPF2 and enhances the SUMOylation of MYC2. Phenotypic analysis revealed that SPF1/SPF2 function redundantly as positive regulators of blue light-mediated photomorphogenesis. Our data demonstrate that SUMO conjugation does not affect the dimerization of MYC transcription factors but modulates the interaction of MYC2 with its cognate DNA cis-element and with the ubiquitin ligase Plant U-box 10 (PUB10). Finally, we show that non-SUMOylatable MYC2 is less stable and interacts more strongly with PUB10 than the WT. Taken together, we conclude that SUMO functions as a counterpoint to the ubiquitin-mediated degradation of MYC2, thereby enhancing its function in blue light signaling.


Asunto(s)
Proteínas de Arabidopsis , Arabidopsis , Arabidopsis/metabolismo , Proteínas de Arabidopsis/metabolismo , Factores de Transcripción Básicos con Cremalleras de Leucinas y Motivos Hélice-Asa-Hélice/metabolismo , Ciclopentanos/metabolismo , Regulación de la Expresión Génica de las Plantas/genética , Plantones/genética , Factores de Transcripción/genética , Factores de Transcripción/metabolismo , Ubiquitinas/genética
2.
Plant Cell Rep ; 40(11): 2047-2061, 2021 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-34129078

RESUMEN

KEY MESSAGE: The intersection of phytohormone signalling pathways with SUMOylation, a key post-translational modification, offers an additional layer of control to the phytohormone signalling for sophisticated regulation of plant development. Plants live in a constantly changing environment that are often challenging for the growth and development of plants. Phytohormones play a critical role in modulating molecular-level changes for enabling plants to resist climatic aberrations. The orchestration of such effective molecular responses entails rapid regulation of phytohormone signalling at transcriptional, translational and post-translational levels. Post-translational modifications have emerged as a key player in modulating hormonal pathways. The current review lays emphasis on the role of SUMOylation, a key post-translational modification, in manipulating individual hormone signalling pathways for better plant adaptability. Here, we discuss the recent advancement in the field and highlights how SUMO targets key signalling intermediates including transcription factors to provide a quick response to different biotic or abiotic stresses, sometimes even prior to changes in hormone levels. The understanding of the convergence of SUMOylation and hormonal pathways will offer an additional layer of control to the phytohormone signalling for an intricate and sophisticated regulation of plant development and can be utilised as a tool to generate climate-resilient crops.


Asunto(s)
Reguladores del Crecimiento de las Plantas/metabolismo , Proteínas de Plantas/metabolismo , Sumoilación , Secuencias de Aminoácidos , Desarrollo de la Planta , Procesamiento Proteico-Postraduccional , Transducción de Señal
3.
Proc Natl Acad Sci U S A ; 118(10)2021 03 09.
Artículo en Inglés | MEDLINE | ID: mdl-33649235

RESUMEN

The versatility of mitogen-activated protein kinases (MAPKs) in translating exogenous and endogenous stimuli into appropriate cellular responses depends on its substrate specificity. In animals, several mechanisms have been proposed about how MAPKs maintain specificity to regulate distinct functional pathways. However, little is known of mechanisms that enable substrate selectivity in plant MAPKs. Small ubiquitin-like modifier (SUMO), a posttranslational modification system, plays an important role in plant development and defense by rapid reprogramming of cellular events. In this study we identified a functional SUMO interaction motif (SIM) in Arabidopsis MPK3 and MPK6 that reveals a mechanism for selective interaction of MPK3/6 with SUMO-conjugated WRKY33, during defense. We show that WRKY33 is rapidly SUMOylated in response to Botrytis cinerea infection and flg22 elicitor treatment. SUMOylation mediates WRKY33 phosphorylation by MPKs and consequent transcription factor activity. Disruption of either WRKY33 SUMO or MPK3/6 SIM sites attenuates their interaction and inactivates WRKY33-mediated defense. However, MPK3/6 SIM mutants show normal interaction with a non-SUMOylated form of another transcription factor, SPEECHLESS, unraveling a role for SUMOylation in differential substrate selectivity by MPKs. We reveal that the SUMO proteases, SUMO PROTEASE RELATED TO FERTILITY1 (SPF1) and SPF2 control WRKY33 SUMOylation and demonstrate a role for these SUMO proteases in defense. Our data reveal a mechanism by which MPK3/6 prioritize molecular pathways by differentially selecting substrates using the SUMO-SIM module during defense responses.


Asunto(s)
Proteínas de Arabidopsis , Arabidopsis , Botrytis/inmunología , Quinasas de Proteína Quinasa Activadas por Mitógenos , Proteínas Quinasas Activadas por Mitógenos , Enfermedades de las Plantas , Ubiquitinas , Arabidopsis/genética , Arabidopsis/inmunología , Arabidopsis/microbiología , Proteínas de Arabidopsis/genética , Proteínas de Arabidopsis/inmunología , Quinasas de Proteína Quinasa Activadas por Mitógenos/genética , Quinasas de Proteína Quinasa Activadas por Mitógenos/inmunología , Proteínas Quinasas Activadas por Mitógenos/genética , Proteínas Quinasas Activadas por Mitógenos/inmunología , Enfermedades de las Plantas/genética , Enfermedades de las Plantas/inmunología , Ubiquitinas/genética , Ubiquitinas/inmunología
5.
Physiol Plant ; 171(1): 77-85, 2021 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-32880960

RESUMEN

Post-translational modifications (PTMs) play a critical role in regulating plant growth and development through the modulation of protein functionality and its interaction with its partners. Analysis of the functional implication of PTMs on plant cellular signalling presents grand challenges in understanding their significance. Proteins decorated or modified with another chemical group or polypeptide play a significant role in regulating physiological processes as compared with non-decorated or non-modified proteins. In the past decade, SUMOylation has been emerging as a potent PTM influencing the adaptability of plants to growth, in response to various environmental cues. Deciphering the SUMO-mediated regulation of plant stress responses and its consequences is required to understand the mechanism underneath. Here, we will discuss the recent advances in the role and significance of SUMOylation in plant growth, development and stress response.


Asunto(s)
Desarrollo de la Planta , Sumoilación , Plantas , Procesamiento Proteico-Postraduccional
6.
Curr Biol ; 30(19): 3880-3888.e5, 2020 10 05.
Artículo en Inglés | MEDLINE | ID: mdl-32795439

RESUMEN

Morphological variation is the basis of natural diversity and adaptation. For example, angiosperms (flowering plants) evolved during the Cretaceous period more than 100 mya and quickly colonized terrestrial habitats [1]. A major reason for their astonishing success was the formation of fruits, which exist in a myriad of different shapes and sizes [2]. Evolution of organ shape is fueled by variation in expression patterns of regulatory genes causing changes in anisotropic cell expansion and division patterns [3-5]. However, the molecular mechanisms that alter the polarity of growth to generate novel shapes are largely unknown. The heart-shaped fruits produced by members of the Capsella genus comprise an anatomical novelty, making it particularly well suited for studies on morphological diversification [6-8]. Here, we show that post-translational modification of regulatory proteins provides a critical step in organ-shape formation. Our data reveal that the SUMO protease, HEARTBREAK (HTB), from Capsella rubella controls the activity of the key regulator of fruit development, INDEHISCENT (CrIND in C. rubella), via de-SUMOylation. This post-translational modification initiates a transduction pathway required to ensure precisely localized auxin biosynthesis, thereby facilitating anisotropic cell expansion to ultimately form the heart-shaped Capsella fruit. Therefore, although variation in the expression of key regulatory genes is known to be a primary driver in morphological evolution, our work demonstrates how other processes-such as post-translational modification of one such regulator-affects organ morphology.


Asunto(s)
Capsella/genética , Frutas/genética , Regulación de la Expresión Génica de las Plantas/genética , Adaptación Fisiológica/genética , Anisotropía , Proteínas de Arabidopsis , Factores de Transcripción con Motivo Hélice-Asa-Hélice Básico/metabolismo , Capsella/crecimiento & desarrollo , Frutas/crecimiento & desarrollo , Expresión Génica/genética , Proteínas de Plantas/metabolismo , Procesamiento Proteico-Postraduccional/genética , Ubiquitinas/genética , Ubiquitinas/metabolismo
7.
Curr Biol ; 30(8): 1410-1423.e3, 2020 04 20.
Artículo en Inglés | MEDLINE | ID: mdl-32109396

RESUMEN

Brassinosteroids (BRs) play crucial roles in plant development, but little is known of mechanisms that integrate environmental cues into BR signaling. Conjugation to the small ubiquitin-like modifier (SUMO) is emerging as an important mechanism to transduce environmental cues into cellular signaling. In this study, we show that SUMOylation of BZR1, a key transcription factor of BR signaling, provides a conduit for environmental influence to modulate growth during stress. SUMOylation stabilizes BZR1 in the nucleus by inhibiting its interaction with BIN2 kinase. During salt stress, Arabidopsis plants arrest growth through deSUMOylation of BZR1 in the cytoplasm by promoting the accumulation of the BZR1 targeting SUMO protease, ULP1a. ULP1a mutants are salt tolerant and insensitive to the BR inhibitor, brassinazole. BR treatment stimulates ULP1a degradation, allowing SUMOylated BZR1 to accumulate and promote growth. This study uncovers a mechanism for integrating environmental cues into BR signaling to shape growth.


Asunto(s)
Proteínas de Arabidopsis/genética , Arabidopsis/genética , Brasinoesteroides/metabolismo , Cisteína Endopeptidasas/genética , Proteínas de Unión al ADN/genética , Transducción de Señal/genética , Arabidopsis/crecimiento & desarrollo , Proteínas de Arabidopsis/metabolismo , Núcleo Celular , Cisteína Endopeptidasas/metabolismo , Proteínas de Unión al ADN/metabolismo , Sumoilación
8.
Front Plant Sci ; 10: 1150, 2019.
Artículo en Inglés | MEDLINE | ID: mdl-31620160

RESUMEN

Efficient elimination of the editing machinery remains a challenge in plant biotechnology after genome editing to minimize the probability of off-target mutations, but it is also important to deliver end users with edited plants free of foreign DNA. Using the modular cloning system Golden Braid, we have included a fluorescence-dependent transgene monitoring module to the genome-editing tool box. We have tested this approach in Solanum lycopersicum, Oryza sativa, and Arabidopsis thaliana. We demonstrate that DsRED fluorescence visualization works efficiently in dry seeds as marker for the detection of the transgene in the three species allowing an efficient method for selecting transgene-free dry seeds. In the first generation of DsRED-free CRISPR/Cas9 null segregants, we detected gene editing of selected targets including homozygous mutants for the plant species tested. We demonstrate that this strategy allows rapid selection of transgene-free homozygous edited crop plants in a single generation after in vitro transformation.

9.
Science ; 362(6421): 1407-1410, 2018 12 21.
Artículo en Inglés | MEDLINE | ID: mdl-30573626

RESUMEN

Plants adapt to heterogeneous soil conditions by altering their root architecture. For example, roots branch when in contact with water by using the hydropatterning response. We report that hydropatterning is dependent on auxin response factor ARF7. This transcription factor induces asymmetric expression of its target gene LBD16 in lateral root founder cells. This differential expression pattern is regulated by posttranslational modification of ARF7 with the small ubiquitin-like modifier (SUMO) protein. SUMOylation negatively regulates ARF7 DNA binding activity. ARF7 SUMOylation is required to recruit the Aux/IAA (indole-3-acetic acid) repressor protein IAA3. Blocking ARF7 SUMOylation disrupts IAA3 recruitment and hydropatterning. We conclude that SUMO-dependent regulation of auxin response controls root branching pattern in response to water availability.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Arabidopsis/crecimiento & desarrollo , Raíces de Plantas/crecimiento & desarrollo , Sumoilación , Factores de Transcripción/metabolismo , Agua/metabolismo , Arabidopsis/genética , Arabidopsis/metabolismo , Proteínas de Arabidopsis/genética , ADN de Plantas/metabolismo , Regulación de la Expresión Génica de las Plantas , Ácidos Indolacéticos/metabolismo , Proteínas Nucleares/metabolismo , Raíces de Plantas/genética , Raíces de Plantas/metabolismo , Unión Proteica , Proteína SUMO-1/metabolismo
10.
Nat Commun ; 9(1): 5185, 2018 12 05.
Artículo en Inglés | MEDLINE | ID: mdl-30518761

RESUMEN

Detection of conserved microbial patterns by host cell surface pattern recognition receptors (PRRs) activates innate immunity. The FLAGELLIN-SENSITIVE 2 (FLS2) receptor perceives bacterial flagellin and recruits another PRR, BAK1 and the cytoplasmic-kinase BIK1 to form an active co-receptor complex that initiates antibacterial immunity in Arabidopsis. Molecular mechanisms that transmit flagellin perception from the plasma-membrane FLS2-associated receptor complex to intracellular events are less well understood. Here, we show that flagellin induces the conjugation of the SMALL UBIQUITIN-LIKE MODIFIER (SUMO) protein to FLS2 to trigger release of BIK1. Disruption of FLS2 SUMOylation can abolish immune responses, resulting in susceptibility to bacterial pathogens in Arabidopsis. We also identify the molecular machinery that regulates FLS2 SUMOylation and demonstrate a role for the deSUMOylating enzyme, Desi3a in innate immunity. Flagellin induces the degradation of Desi3a and enhances FLS2 SUMOylation to promote BIK1 dissociation and trigger intracellular immune signalling.


Asunto(s)
Proteínas de Arabidopsis/inmunología , Arabidopsis/inmunología , Cisteína Endopeptidasas/inmunología , Enfermedades de las Plantas/inmunología , Proteínas Quinasas/inmunología , Pseudomonas syringae/inmunología , Receptores de Reconocimiento de Patrones/inmunología , Arabidopsis/genética , Arabidopsis/microbiología , Proteínas de Arabidopsis/genética , Proteínas Bacterianas/inmunología , Cisteína Endopeptidasas/genética , Flagelina/inmunología , Inmunidad Innata , Enfermedades de las Plantas/microbiología , Proteínas Quinasas/genética , Proteínas Serina-Treonina Quinasas/genética , Proteínas Serina-Treonina Quinasas/inmunología , Pseudomonas syringae/genética , Pseudomonas syringae/fisiología , Receptores de Reconocimiento de Patrones/genética , Transducción de Señal , Sumoilación
12.
Plant Cell ; 30(9): 2099-2115, 2018 09.
Artículo en Inglés | MEDLINE | ID: mdl-30115737

RESUMEN

Plants respond rapidly to sudden environmental cues, often responding prior to changes in the hormone levels that coordinate these responses. How this is achieved is not fully understood. The integrative role of the phytohormone jasmonic acid (JA) relies upon the plant's ability to control the levels of JASMONATE ZIM (JAZ) domain-containing repressor proteins. Here, we demonstrate that regardless of intrinsic JA levels, Small Ubiquitin-like Modifier (SUMO)-conjugated JAZ proteins inhibit the JA receptor CORONATINE INSENSITIVE1 (COI1) from mediating non-SUMOylated JAZ degradation. The SUMO-deconjugating proteases OVERLY TOLERANT TO SALT1 (OTS1) and OTS2 regulate JAZ protein SUMOylation and stability. The ots1 ots2 double mutants accumulate SUMOylated and non-SUMOylated JAZ repressor proteins but show no change in endogenous JA levels compared with wild-type plants. SUMO1-conjugated JAZ proteins bind to COI1 independently of the JA mimic coronatine. SUMO inhibits JAZ binding to COI1. We identify the SUMO interacting motif in COI1 and demonstrate that this is vital to SUMO-dependent inhibition of COI1. Necrotroph infection of Arabidopsis thaliana promotes SUMO protease degradation, and this increases JAZ SUMOylation and abundance, which in turn inhibits JA signaling. This study reveals a mechanism for rapidly regulating JA responses, allowing plants to adapt to environmental changes.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Ubiquitinas/metabolismo , Proteínas de Arabidopsis/genética , Ciclopentanos/metabolismo , Cisteína Endopeptidasas/genética , Cisteína Endopeptidasas/metabolismo , Regulación de la Expresión Génica de las Plantas/genética , Regulación de la Expresión Génica de las Plantas/fisiología , Oxilipinas/metabolismo , Transducción de Señal , Ubiquitinas/genética
13.
J Exp Bot ; 69(19): 4625-4632, 2018 08 31.
Artículo en Inglés | MEDLINE | ID: mdl-29897480

RESUMEN

In recent years, post-translational modification (PTM) of proteins has emerged as a key process that integrates plant growth and response to a changing environment. During the processes of domestication and breeding, plants were selected for various yield and adaptational characteristics. The post-translational modifier small ubiquitin-like modifier (SUMO) protein is known to have a role in the regulation of a number of these characteristics. Using bioinformatics, we mined the genomes of cereal and Brassica crops and their non-crop relatives Arabidopsis thaliana and Brachypodium distachyon for ubiquitin-like protease (ULP) SUMO protease sequences. We discovered that the SUMO system in cereal crops is disproportionately elaborate in comparison with that in B. distachyon. We use these data to propose deSUMOylation as a mechanism for specificity in the SUMO system.


Asunto(s)
Producción de Cultivos , Productos Agrícolas/fisiología , Péptido Hidrolasas/genética , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/genética , Sumoilación , Arabidopsis/genética , Arabidopsis/metabolismo , Brachypodium/genética , Brachypodium/metabolismo , Biología Computacional , Productos Agrícolas/genética , Productos Agrícolas/crecimiento & desarrollo , Péptido Hidrolasas/metabolismo , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/metabolismo
14.
Plant J ; 92(6): 1031-1043, 2017 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-29024118

RESUMEN

Conjugation of SUMO (Small Ubiquitin-like Modifier) protein to cellular targets is emerging as a very influential protein modification system. Once covalently bound, SUMO conjugation can change the stability or functionality of its cognate target proteins. SUMO protease can rapidly reverse SUMO conjugation making this modification system highly dynamic. A major factor in the variation of SUMO-target function is the balance between the conjugated/de-conjugated forms. The mechanistic role of these regulatory SUMO proteases in mediating stress responses has not been defined in any crops. In this study, we reveal the role of the SUMO protease, OsOTS1 in mediating tolerance to drought in rice. OsOTS1 depleted transgenic plants accumulate more ABA and exhibit more productive agronomic traits during drought while OsOTS1 overexpressing lines are drought sensitive but ABA insensitive. Drought and ABA treatment stimulates the degradation of OsOTS1 protein indicating that SUMO conjugation is an important response to drought stress in rice achieved through down-regulation of OTS1/2 activity. We reveal that OsOTS1 SUMO protease directly targets the ABA and drought responsive transcription factor OsbZIP23 for de-SUMOylation affecting its stability. OsOTS-RNAi lines show increased abundance of OsbZIP23 and increased drought responsive gene expression while OsOTS1 overexpressing lines show reduced levels of OsbZIP23 leading to suppressed drought responsive gene expression. Our data reveal a mechanism in which rice plants govern ABA-dependant drought responsive gene expression by controlling the stability of OsbZIP23 by SUMO conjugation through manipulating specific SUMO protease levels.


Asunto(s)
Ácido Abscísico/metabolismo , Oryza/genética , Reguladores del Crecimiento de las Plantas/metabolismo , Proteínas de Plantas/metabolismo , Transducción de Señal , Factores de Transcripción con Cremalleras de Leucina de Carácter Básico/genética , Factores de Transcripción con Cremalleras de Leucina de Carácter Básico/metabolismo , Sequías , Regulación de la Expresión Génica de las Plantas , Modelos Biológicos , Oryza/enzimología , Oryza/fisiología , Péptido Hidrolasas/genética , Péptido Hidrolasas/metabolismo , Proteínas de Plantas/genética , Plantas Modificadas Genéticamente , Proteolisis , Interferencia de ARN , Salinidad , Estrés Fisiológico , Sumoilación , Técnicas del Sistema de Dos Híbridos , Ubiquitinas/genética , Ubiquitinas/metabolismo
15.
Methods Mol Biol ; 1450: 125-33, 2016.
Artículo en Inglés | MEDLINE | ID: mdl-27424750

RESUMEN

The conjugation of SUMO can profoundly change the behavior of substrate proteins, impacting a wide variety of cellular responses. SUMO proteases are emerging as key regulators of plant adaptation to its environment because of their instrumental role in the SUMO deconjugation process. Here, we describe how to express, purify, and determine SUMO deconjugation activity of a plant SUMO protease.


Asunto(s)
Biología Molecular/métodos , Péptido Hidrolasas/aislamiento & purificación , Plantas/química , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/aislamiento & purificación , Regulación de la Expresión Génica de las Plantas , Péptido Hidrolasas/química , Péptido Hidrolasas/genética , Plantas/genética , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/química , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/genética
16.
Plant Signal Behav ; 11(5): e1173301, 2016 05 03.
Artículo en Inglés | MEDLINE | ID: mdl-27119209

RESUMEN

Salinity is one of the major environmental stresses affecting rice production worldwide. Improving rice salt tolerance is a critical step for sustainable food production. Posttranslational modifications of proteins greatly expand proteome diversity, increase functionality and allow quick responses to environmental stresses, all at low cost to the cell. SUMO mediated modification of substrate proteins is a highly dynamic process governed by the balance of activities of SUMO E3 ligases and deconjugating SUMO proteases. In recent years, SUMO (Small Ubiquitin like Modifier) conjugation of proteins has emerged as an influential regulator of stress signaling in the model plant Arabidopsis. However SUMOylation remain largely under studied in crop plants. We recently identified the SUMO protease gene family in rice and demonstrated a role for OsOTS1 SUMO proteases in salt stress. Interestingly, rice plants silencing OsOTS1 also show significantly reduced germination rate. Knockdown of OsOTS1 gene expression affects root growth by primarily reducing cell size rather than cell division.


Asunto(s)
Germinación/efectos de los fármacos , Oryza/crecimiento & desarrollo , Péptido Hidrolasas/metabolismo , Proteínas de Plantas/metabolismo , Raíces de Plantas/crecimiento & desarrollo , Tolerancia a la Sal/efectos de los fármacos , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/metabolismo , Cloruro de Sodio/farmacología , Tamaño de la Célula/efectos de los fármacos , Oryza/citología , Oryza/efectos de los fármacos , Oryza/fisiología , Raíces de Plantas/citología , Raíces de Plantas/efectos de los fármacos , Plantas Modificadas Genéticamente , Interferencia de ARN , Estrés Fisiológico
17.
J Exp Bot ; 67(9): 2541-8, 2016 04.
Artículo en Inglés | MEDLINE | ID: mdl-27012284

RESUMEN

Plants have evolved to cope with changing environmental conditions. One way plants achieve this is through post-translational modification of target proteins by ubiquitination and SUMOylation. These post-translational modifiers (PMs) can alter stability, protein-protein interactions, and the overall fate of the protein. Both of these systems have remarkable similarities in terms of the process leading to attachment of the PM to its substrate : having to undertake activation, conjugation, and finally ligation to the target. In the ubiquitin system, there are a vast number of ubiquitin ligase enzymes (E3s) that provide specificity for the attachment of ubiquitin. With the SUMO system, only a small number of SUMO E3 ligases have so far been identified in the fully sequenced plant genomes. In Arabidopsis thaliana, there are only two SUMO E3s, compared to over 1400 ubiquitin E3s, a trend also observed in crop species such as Oryza sativa and Zea mays Recent research indicates that removing SUMO from its substrate by the enzymatically active SUMO proteases is a vital part of this system. A class of SUMO proteases called ubiquitin-like proteases (ULPs) are widespread in all eukaryotes; within plants, both monocot and dicot kingdoms have conserved and divergent ULPs and ULP-like proteases. This paper examines the roles ULPs have in stress responses and highlights the 'fine-tuning' of SUMO attachment/removal in balancing growth versus stress.


Asunto(s)
Plantas/enzimología , Procesamiento Proteico-Postraduccional , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/metabolismo , Sumoilación , Proteasas Ubiquitina-Específicas/metabolismo , Plantas/metabolismo , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/fisiología , Sumoilación/fisiología , Proteasas Ubiquitina-Específicas/fisiología
18.
Plant Physiol ; 170(4): 2378-91, 2016 04.
Artículo en Inglés | MEDLINE | ID: mdl-26869703

RESUMEN

SUMO (Small Ubiquitin-like Modifier) conjugation onto target proteins has emerged as a very influential class of protein modification systems. SUMO1/2 double mutant plants are nonviable, underlining the importance of SUMO conjugation to plant survival. Once covalently bound, SUMO can alter a conjugated protein's stability and/or function. SUMO conjugation is a highly dynamic process that can be rapidly reversed by the action of SUMO proteases. The balance between the conjugated/deconjugated forms is a major determinant in the modulation of SUMO-target function. Despite the important mechanistic role of SUMO proteases in model plants, until now the identity or the function of these regulatory enzymes has not been defined in any crop plant. In this report, we reveal the ubiquitin-like protease class of SUMO protease gene family in rice (Oryza sativa) and demonstrate a critical role for OsOTS1 SUMO protease in salt stress. OsOTS-RNAi rice plants accumulate high levels of SUMO-conjugated proteins during salt stress and are highly salt sensitive; however, in non-salt conditions, they are developmentally indistinguishable from wild-type plants. Transgenic rice plants overexpressing OsOTS1 have increased salt tolerance and a concomitant reduction in the levels of SUMOylated proteins. We demonstrate that OsOTS1 confers salt tolerance in rice by increasing root biomass. High salinity triggers OsOTS1 degradation, indicating that increased SUMO conjugation in rice plants during salt stress is in part achieved by down-regulation of OTS1/2 activity. OsOTS1 is nuclear localized indicating a direct requirement of OsOTS1-dependent deSUMOylation activity in rice nuclei for salt tolerance.


Asunto(s)
Oryza/fisiología , Proteínas de Plantas/metabolismo , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/metabolismo , Cloruro de Sodio/farmacología , Estrés Fisiológico/efectos de los fármacos , Secuencia de Aminoácidos , Clorofila/metabolismo , Regulación de la Expresión Génica de las Plantas/efectos de los fármacos , Genes de Plantas , Proteínas Nucleares/metabolismo , Oryza/efectos de los fármacos , Oryza/genética , Fenotipo , Filogenia , Proteínas de Plantas/química , Proteínas de Plantas/genética , Raíces de Plantas/efectos de los fármacos , Raíces de Plantas/genética , Raíces de Plantas/crecimiento & desarrollo , Plantas Modificadas Genéticamente , Proteolisis/efectos de los fármacos , Interferencia de ARN , Tolerancia a la Sal/efectos de los fármacos , Alineación de Secuencia , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/química , Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina/genética , Suelo , Fracciones Subcelulares/efectos de los fármacos , Fracciones Subcelulares/metabolismo , Sumoilación/efectos de los fármacos , Regulación hacia Arriba/efectos de los fármacos , Regulación hacia Arriba/genética
19.
J Exp Bot ; 67(1): 353-63, 2016 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-26494731

RESUMEN

Small ubiquitin-like modifier proteases 1 and 2 (SUMO1/2) have been linked to the regulation of salicylic acid (SA)-mediated defence signalling in Arabidopsis thaliana. In order to define the role of the SUMO proteases OVERLY TOLERANT TO SALT1 and -2 (OTS1/2) in defence and to provide insight into SUMO1/2-mediated regulation of SA signalling, we examined the status of SA-mediated defences in ots1/2 mutants. The ots1 ots2 double mutant displayed enhanced resistance to virulent Pseudomonas syringae and higher levels of SA compared with wild-type (WT) plants. Furthermore, ots1 ots2 mutants exhibited upregulated expression of the SA biosynthesis gene ICS1 in addition to enhanced SA-responsive ICS1 expression beyond that of WT. SA stimulated OTS1/2 degradation and promoted accumulation of SUMO1/2 conjugates. These results indicate that OTS1 and -2 act in a feedback loop in SA signalling and that de novo OTS1/2 synthesis works antagonistically to SA-promoted degradation, adjusting the abundance of OTS1/2 to moderate SA signalling. Accumulation of SUMO1/2 conjugates coincides with SA-promoted OTS degradation and may play a positive role in SA-mediated signalling in addition to its repressive roles reported elsewhere.


Asunto(s)
Proteínas de Arabidopsis/genética , Arabidopsis/genética , Cisteína Endopeptidasas/genética , Regulación de la Expresión Génica de las Plantas , Pseudomonas syringae/fisiología , Ácido Salicílico/metabolismo , Arabidopsis/metabolismo , Arabidopsis/microbiología , Proteínas de Arabidopsis/metabolismo , Cisteína Endopeptidasas/metabolismo , Enfermedades de las Plantas/inmunología , Inmunidad de la Planta , Transducción de Señal
20.
Plant Physiol ; 169(4): 2922-34, 2015 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-26474641

RESUMEN

Arabidopsis (Arabidopsis thaliana) Short Hypocotyl in White Light1 (SHW1) encodes a Ser-Arg-Asp-rich protein that acts as a negative regulator of photomorphogenesis. SHW1 and Constitutive Photomorphogenic1 (COP1) genetically interact in an additive manner to suppress photomorphogenesis. Elongated Hypocotyl5 (HY5) is a photomorphogenesis promoting a basic leucine zipper transcription factor that is degraded by COP1 ubiquitin ligase in the darkness. Here, we report the functional interrelation of SHW1 with COP1 and HY5 in Arabidopsis seedling development. The in vitro and in vivo molecular interaction studies show that SHW1 physically interacts with both COP1 and HY5. The genetic studies reveal that SHW1 and HY5 work in an antagonistic manner to regulate photomorphogenic growth. Additional mutation of SHW1 in hy5 mutant background is able to suppress the gravitropic root growth defect of hy5 mutants. This study further reveals that the altered abscisic acid responsiveness of hy5 mutants is modulated by additional loss of SHW1 function. Furthermore, this study shows that SHW1 promotes COP1-mediated degradation of HY5 through enhanced ubiquitylation in the darkness. Collectively, this study highlights a mechanistic view on coordinated regulation of SHW1, COP1, and HY5 in Arabidopsis seedling development.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Arabidopsis/metabolismo , Factores de Transcripción con Cremalleras de Leucina de Carácter Básico/metabolismo , Proteínas Nucleares/metabolismo , Plantones/metabolismo , Ácido Abscísico/farmacología , Arabidopsis/genética , Arabidopsis/crecimiento & desarrollo , Proteínas de Arabidopsis/genética , Factores de Transcripción con Cremalleras de Leucina de Carácter Básico/genética , Western Blotting , Regulación de la Expresión Génica de las Plantas/efectos de los fármacos , Regulación de la Expresión Génica de las Plantas/efectos de la radiación , Luz , Mutación , Proteínas Nucleares/genética , Organogénesis de las Plantas/efectos de los fármacos , Organogénesis de las Plantas/genética , Organogénesis de las Plantas/efectos de la radiación , Reguladores del Crecimiento de las Plantas/farmacología , Unión Proteica , Proteolisis , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Plantones/genética , Plantones/crecimiento & desarrollo , Técnicas del Sistema de Dos Híbridos , Ubiquitina-Proteína Ligasas , Ubiquitinación/efectos de los fármacos , Ubiquitinación/efectos de la radiación
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