Novel players fine-tune plant trade-offs

2015 ◽  
Vol 58 ◽  
pp. 83-100 ◽  
Author(s):  
Selena Gimenez-Ibanez ◽  
Marta Boter ◽  
Roberto Solano

Jasmonates (JAs) are essential signalling molecules that co-ordinate the plant response to biotic and abiotic challenges, as well as co-ordinating several developmental processes. Huge progress has been made over the last decade in understanding the components and mechanisms that govern JA perception and signalling. The bioactive form of the hormone, (+)-7-iso-jasmonyl-l-isoleucine (JA-Ile), is perceived by the COI1–JAZ co-receptor complex. JASMONATE ZIM DOMAIN (JAZ) proteins also act as direct repressors of transcriptional activators such as MYC2. In the emerging picture of JA-Ile perception and signalling, COI1 operates as an E3 ubiquitin ligase that upon binding of JA-Ile targets JAZ repressors for degradation by the 26S proteasome, thereby derepressing transcription factors such as MYC2, which in turn activate JA-Ile-dependent transcriptional reprogramming. It is noteworthy that MYCs and different spliced variants of the JAZ proteins are involved in a negative regulatory feedback loop, which suggests a model that rapidly turns the transcriptional JA-Ile responses on and off and thereby avoids a detrimental overactivation of the pathway. This chapter highlights the most recent advances in our understanding of JA-Ile signalling, focusing on the latest repertoire of new targets of JAZ proteins to control different sets of JA-Ile-mediated responses, novel mechanisms of negative regulation of JA-Ile signalling, and hormonal cross-talk at the molecular level that ultimately determines plant adaptability and survival.

2020 ◽  
Vol 64 (3) ◽  
pp. 501-512
Author(s):  
Gareth Griffiths

Abstract Jasmonates (JAs) are physiologically important molecules involved in a wide range of plant responses from growth, flowering, senescence to defence against abiotic and biotic stress. They are rapidly synthesised from α-linolenic acid (ALA; C18:3 ∆9,12,15) by a process of oxidation, cyclisation and acyl chain shortening involving co-operation between the chloroplast and peroxisome. The active form of JA is the isoleucine conjugate, JA-isoleucine (JA-Ile), which is synthesised in the cytoplasm. Other active metabolites of JA include the airborne signalling molecules, methyl JA (Me-JA) and cis-jasmone (CJ), which act as inter-plant signalling molecules activating defensive genes encoding proteins and secondary compounds such as anthocyanins and alkaloids. One of the key defensive metabolites in many plants is a protease inhibitor that inactivates the protein digestive capabilities of insects, thereby, reducing their growth. The receptor for JA-Ile is a ubiquitin ligase termed as SCFCoi1 that targets the repressor protein JA Zim domain (JAZ) for degradation in the 26S proteasome. Removal of JAZ allows other transcription factors (TFs) to activate the JA response. The levels of JA-Ile are controlled through catabolism by hydroxylating enzymes of the cytochrome P450 (CYP) family. The JAZ proteins act as metabolic hubs and play key roles in cross-talk with other phytohormone signalling pathways in co-ordinating genome-wide responses. Specific subsets of JAZ proteins are involved in regulating different response outcomes such as growth inhibition versus biotic stress responses. Understanding the molecular circuits that control plant responses to pests and pathogens is a necessary pre-requisite to engineering plants with enhanced resilience to biotic challenges for improved agricultural yields.


2021 ◽  
Author(s):  
Ruben Ceulemans ◽  
Laurie Anne Myriam Wojcik ◽  
Ursula Gaedke

Biodiversity decline causes a loss of functional diversity, which threatens ecosystems through a dangerous feedback loop: this loss may hamper ecosystems' ability to buffer environmental changes, leading to further biodiversity losses. In this context, the increasing frequency of climate and human-induced excessive loading of nutrients causes major problems in aquatic systems. Previous studies investigating how functional diversity influences the response of food webs to disturbances have mainly considered systems with at most two functionally diverse trophic levels. Here, we investigate the effects of a nutrient pulse on the resistance, resilience and elasticity of a tritrophic---and thus more realistic---plankton food web model depending on its functional diversity. We compare a non-adaptive food chain with no diversity to a highly diverse food web with three adaptive trophic levels. The species fitness differences are balanced through trade-offs between defense/growth rate for prey and selectivity/half-saturation constant for predators. We showed that the resistance, resilience and elasticity of tritrophic food webs decreased with larger perturbation sizes and depended on the state of the system when the perturbation occured. Importantly, we found that a more diverse food web was generally more resistant, resilient, and elastic. Particularly, functional diversity dampened the probability of a regime shift towards a non-desirable alternative state. In addition, despite the complex influence of the shape and type of the dynamical attractors, the basal-intermediate interaction determined the robustness against a nutrient pulse. This relationship was strongly influenced by the diversity present and the third trophic level. Overall, using a food web model of realistic complexity, this study confirms the destructive potential of the positive feedback loop between biodiversity loss and robustness, by uncovering mechanisms leading to a decrease in resistance, resilience and elasticity as functional diversity declines.


2017 ◽  
Vol 28 (21) ◽  
pp. 2819-2832 ◽  
Author(s):  
Christos Gournas ◽  
Elie Saliba ◽  
Eva-Maria Krammer ◽  
Céline Barthelemy ◽  
Martine Prévost ◽  
...  

Substrate-transport–elicited endocytosis is a common control mechanism of membrane transporters avoiding excess uptake of external compounds, though poorly understood at the molecular level. In yeast, endocytosis of transporters is triggered by their ubiquitylation mediated by the Rsp5 ubiquitin-ligase, recruited by α-arrestin–family adaptors. We here report that transport-elicited ubiquitylation of the arginine transporter Can1 is promoted by transition to an inward-facing state. This conformational change unveils a region of the N-terminal cytosolic tail targeted by the Art1 α-arrestin, which is activated via the TORC1 kinase complex upon arginine uptake. Can1 mutants altered in the arginine-binding site or a cytosolic tripeptide sequence permanently expose the α-arrestin–targeted region so that Art1 activation via TORC1 is sufficient to trigger their endocytosis. We also provide evidence that substrate-transport elicited endocytosis of other amino acid permeases similarly involves unmasking of a cytosolic Art1-target region coupled to activation of Art1 via TORC1. Our results unravel a mechanism likely involved in regulation of many other transporters by their own substrates. They also support the emerging view that transporter ubiquitylation relies on combinatorial interaction rules such that α-arrestins, stimulated via signaling cascades or in their basal state, recognize transporter regions permanently facing the cytosol or unveiled during transport.


2001 ◽  
Vol 183 (20) ◽  
pp. 5974-5981 ◽  
Author(s):  
Natividad Ruiz ◽  
Celeste N. Peterson ◽  
Thomas J. Silhavy

ABSTRACT The stationary-phase response exhibited by Escherichia coli upon nutrient starvation is mainly induced by a decrease of the ClpXP-dependent degradation of the alternate primary ς factor RpoS. Although it is known that the specific regulation of this proteolysis is exercised by the orphan response regulator SprE, it remains unclear how SprE's activity is regulated in vivo. Previous studies have demonstrated that the cellular content of SprE itself is paradoxically increased in stationary-phase cells in an RpoS-dependent fashion. We show here that this RpoS-dependent upregulation of SprE levels is due to increased transcription. Furthermore, we demonstrate that sprE is part of the two-generssA-sprE operon, but it can also be transcribed from an additional RpoS-dependent promoter located in therssA-sprE intergenic region. In addition, by using an in-frame deletion in rssA we found that RssA does not regulate either SprE or RpoS under the conditions tested.


mBio ◽  
2018 ◽  
Vol 9 (3) ◽  
Author(s):  
Leandro José de Assis ◽  
Mevlut Ulas ◽  
Laure Nicolas Annick Ries ◽  
Nadia Ali Mohamed El Ramli ◽  
Ozlem Sarikaya-Bayram ◽  
...  

ABSTRACTThe attachment of one or more ubiquitin molecules by SCF (Skp–Cullin–F-box) complexes to protein substrates targets them for subsequent degradation by the 26S proteasome, allowing the control of numerous cellular processes. Glucose-mediated signaling and subsequent carbon catabolite repression (CCR) are processes relying on the functional regulation of target proteins, ultimately controlling the utilization of this carbon source. In the filamentous fungusAspergillus nidulans, CCR is mediated by the transcription factor CreA, which modulates the expression of genes encoding biotechnologically relevant enzymes. Although CreA-mediated repression of target genes has been extensively studied, less is known about the regulatory pathways governing CCR and this work aimed at further unravelling these events. The Fbx23 F-box protein was identified as being involved in CCR and the Δfbx23mutant presented impaired xylanase production under repressing (glucose) and derepressing (xylan) conditions. Mass spectrometry showed that Fbx23 is part of an SCF ubiquitin ligase complex that is bridged via the GskA protein kinase to the CreA-SsnF-RcoA repressor complex, resulting in the degradation of the latter under derepressing conditions. Upon the addition of glucose, CreA dissociates from the ubiquitin ligase complex and is transported into the nucleus. Furthermore, casein kinase is important for CreA function during glucose signaling, although the exact role of phosphorylation in CCR remains to be determined. In summary, this study unraveled novel mechanistic details underlying CreA-mediated CCR and provided a solid basis for studying additional factors involved in carbon source utilization which could prove useful for biotechnological applications.IMPORTANCEThe production of biofuels from plant biomass has gained interest in recent years as an environmentally friendly alternative to production from petroleum-based energy sources. Filamentous fungi, which naturally thrive on decaying plant matter, are of particular interest for this process due to their ability to secrete enzymes required for the deconstruction of lignocellulosic material. A major drawback in fungal hydrolytic enzyme production is the repression of the corresponding genes in the presence of glucose, a process known as carbon catabolite repression (CCR). This report provides previously unknown mechanistic insights into CCR through elucidating part of the protein-protein interaction regulatory system that governs the CreA transcriptional regulator in the reference organismAspergillus nidulansin the presence of glucose and the biotechnologically relevant plant polysaccharide xylan.


2020 ◽  
Vol 104 (2) ◽  
pp. 377-390
Author(s):  
Zhaoqing Song ◽  
Tingting Yan ◽  
Jiujie Liu ◽  
Yeting Bian ◽  
Yueqin Heng ◽  
...  
Keyword(s):  

2014 ◽  
Vol 42 (19) ◽  
pp. 12041-12051 ◽  
Author(s):  
Jing-Jing Liu ◽  
Xue-Jia Lin ◽  
Xiao-Jing Yang ◽  
Liangji Zhou ◽  
Shuai He ◽  
...  

2006 ◽  
Vol 20 (8) ◽  
pp. 1715-1727 ◽  
Author(s):  
Laurence Canaple ◽  
Juliette Rambaud ◽  
Ouria Dkhissi-Benyahya ◽  
Béatrice Rayet ◽  
Nguan Soon Tan ◽  
...  

Abstract Recent evidence has emerged that peroxisome proliferator-activated receptor α (PPARα), which is largely involved in lipid metabolism, can play an important role in connecting circadian biology and metabolism. In the present study, we investigated the mechanisms by which PPARα influences the pacemakers acting in the central clock located in the suprachiasmatic nucleus and in the peripheral oscillator of the liver. We demonstrate that PPARα plays a specific role in the peripheral circadian control because it is required to maintain the circadian rhythm of the master clock gene brain and muscle Arnt-like protein 1 (bmal1) in vivo. This regulation occurs via a direct binding of PPARα on a potential PPARα response element located in the bmal1 promoter. Reversely, BMAL1 is an upstream regulator of PPARα gene expression. We further demonstrate that fenofibrate induces circadian rhythm of clock gene expression in cell culture and up-regulates hepatic bmal1 in vivo. Together, these results provide evidence for an additional regulatory feedback loop involving BMAL1 and PPARα in peripheral clocks.


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