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1.
Plant Cell ; 34(1): 10-52, 2022 01 20.
Article En | MEDLINE | ID: mdl-34633455

In this glossary of plant cell structures, we asked experts to summarize a present-day view of plant organelles and structures, including a discussion of outstanding questions. In the following short reviews, the authors discuss the complexities of the plant cell endomembrane system, exciting connections between organelles, novel insights into peroxisome structure and function, dynamics of mitochondria, and the mysteries that need to be unlocked from the plant cell wall. These discussions are focused through a lens of new microscopy techniques. Advanced imaging has uncovered unexpected shapes, dynamics, and intricate membrane formations. With a continued focus in the next decade, these imaging modalities coupled with functional studies are sure to begin to unravel mysteries of the plant cell.


Cell Membrane/metabolism , Cell Wall/metabolism , Mitochondria/metabolism , Peroxisomes/metabolism , Plants/metabolism , Organelles/metabolism , Plant Cells/metabolism
2.
Plant Cell ; 33(7): 2431-2453, 2021 08 13.
Article En | MEDLINE | ID: mdl-33944955

Endoplasmic reticulum-plasma membrane contact sites (ER-PM CS) play fundamental roles in all eukaryotic cells. Arabidopsis thaliana mutants lacking the ER-PM protein tether synaptotagmin1 (SYT1) exhibit decreased PM integrity under multiple abiotic stresses, such as freezing, high salt, osmotic stress, and mechanical damage. Here, we show that, together with SYT1, the stress-induced SYT3 is an ER-PM tether that also functions in maintaining PM integrity. The ER-PM CS localization of SYT1 and SYT3 is dependent on PM phosphatidylinositol-4-phosphate and is regulated by abiotic stress. Lipidomic analysis revealed that cold stress increased the accumulation of diacylglycerol at the PM in a syt1/3 double mutant relative to wild-type while the levels of most glycerolipid species remain unchanged. In addition, the SYT1-green fluorescent protein fusion preferentially binds diacylglycerol in vivo with little affinity for polar glycerolipids. Our work uncovers a SYT-dependent mechanism of stress adaptation counteracting the detrimental accumulation of diacylglycerol at the PM produced during episodes of abiotic stress.


Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Cell Membrane/metabolism , Diglycerides/metabolism , Endoplasmic Reticulum/metabolism , Phosphatidylinositol Phosphates/metabolism
3.
Plant Physiol ; 185(3): 650-662, 2021 04 02.
Article En | MEDLINE | ID: mdl-33793898

A vast majority of cellular processes take root at the surface of biological membranes. By providing a two-dimensional platform with limited diffusion, membranes are, by nature, perfect devices to concentrate signaling and metabolic components. As such, membranes often act as "key processors" of cellular information. Biological membranes are highly dynamic and deformable and can be shaped into curved, tubular, or flat conformations, resulting in differentiated biophysical properties. At membrane contact sites, membranes from adjacent organelles come together into a unique 3D configuration, forming functionally distinct microdomains, which facilitate spatially regulated functions, such as organelle communication. Here, we describe the diversity of geometries of contact site-forming membranes in different eukaryotic organisms and explore the emerging notion that their shape, 3D architecture, and remodeling jointly define their cellular activity. The review also provides selected examples highlighting changes in membrane contact site architecture acting as rapid and local responses to cellular perturbations, and summarizes our current understanding of how those structural changes confer functional specificity to those cellular territories.


Cell Membrane/metabolism , Endoplasmic Reticulum/metabolism , Mitochondrial Membranes/metabolism , Signal Transduction/physiology , Plant Physiological Phenomena
5.
Front Cell Dev Biol ; 8: 675, 2020.
Article En | MEDLINE | ID: mdl-32793605

Membrane contact sites between the cortical endoplasmic reticulum (ER) and the plasma membrane (PM) provide a direct conduit for small molecule transfer and signaling between the two largest membranes of the cell. Contact is established through ER integral membrane proteins that physically tether the two membranes together, though the general mechanism is remarkably non-specific given the diversity of different tethering proteins. Primary tethers including VAMP-associated proteins (VAPs), Anoctamin/TMEM16/Ist2p homologs, and extended synaptotagmins (E-Syts), are largely conserved in most eukaryotes and are both necessary and sufficient for establishing ER-PM association. In addition, other species-specific ER-PM tether proteins impart unique functional attributes to both membranes at the cell cortex. This review distils recent functional and structural findings about conserved and species-specific tethers that form ER-PM contact sites, with an emphasis on their roles in the coordinate regulation of lipid metabolism, cellular structure, and responses to membrane stress.

6.
J Exp Bot ; 71(14): 3986-3998, 2020 07 06.
Article En | MEDLINE | ID: mdl-32179893

In plant cells, environmental stressors promote changes in connectivity between the cortical endoplasmic reticulum (ER) and the plasma membrane (PM). Although this process is tightly regulated in space and time, the molecular signals and structural components mediating these changes in interorganelle communication are only starting to be characterized. In this report, we confirm the presence of a putative tethering complex containing the synaptotagmins 1 and 5 (SYT1 and SYT5) and the Ca2+- and lipid-binding protein 1 (CLB1/SYT7). This complex is enriched at ER-PM contact sites (EPCSs), has slow responses to changes in extracellular Ca2+, and displays severe cytoskeleton-dependent rearrangements in response to the trivalent lanthanum (La3+) and gadolinium (Gd3+) rare earth elements (REEs). Although REEs are generally used as non-selective cation channel blockers at the PM, here we show that the slow internalization of REEs into the cytosol underlies the activation of the Ca2+/calmodulin intracellular signaling, the accumulation of phosphatidylinositol-4-phosphate (PI4P) at the PM, and the cytoskeleton-dependent rearrangement of the SYT1/SYT5 EPCS complexes. We propose that the observed EPCS rearrangements act as a slow adaptive response to sustained stress conditions, and that this process involves the accumulation of stress-specific phosphoinositide species at the PM.


Arabidopsis Proteins , Arabidopsis , Arabidopsis/genetics , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Cell Membrane/metabolism , Cytoskeleton/metabolism , Endoplasmic Reticulum/metabolism , Gadolinium , Lanthanum , Synaptotagmin I
7.
Front Plant Sci ; 10: 872, 2019.
Article En | MEDLINE | ID: mdl-31333708

Abscisic acid (ABA) is a plant hormone that can mitigate heavy metal toxicity. Exogenous ABA and ABA mimic 1 (AM1) were applied to study the influence on Zn uptake and accumulation in Vitis vinifera L. cv. Merlot seedlings exposed to excess Zn. The seedlings were treated with either normal or excess levels of Zn in combination with applications of ABA and AM1. Excess Zn exposure resulted in decreased lateral root length, decreased photosynthesis, elevated uptake, and accumulation of Zn in roots, trunks, and stems, decreased jasmonic acid content in roots and leaves, and induced the expression of Zn transportation- and detoxification-related genes. Remarkably, in the presence of toxic amounts of Zn, the exogenous application of ABA, but not of AM1, reduced the uptake and accumulation of Zn in roots and induced higher expression of both ZIP genes and detoxification-related genes in root and leaf. These results indicate that exogenous ABA enhances the tolerance of grape seedlings to excess Zn and that AM1 is not a suitable ABA mimic compound for Zn stress alleviation in grapes.

8.
Proc Natl Acad Sci U S A ; 116(4): 1420-1429, 2019 01 22.
Article En | MEDLINE | ID: mdl-30610176

The interorganelle communication mediated by membrane contact sites (MCSs) is an evolutionary hallmark of eukaryotic cells. MCS connections enable the nonvesicular exchange of information between organelles and allow them to coordinate responses to changing cellular environments. In plants, the importance of MCS components in the responses to environmental stress has been widely established, but the molecular mechanisms regulating interorganelle connectivity during stress still remain opaque. In this report, we use the model plant Arabidopsis thaliana to show that ionic stress increases endoplasmic reticulum (ER)-plasma membrane (PM) connectivity by promoting the cortical expansion of synaptotagmin 1 (SYT1)-enriched ER-PM contact sites (S-EPCSs). We define differential roles for the cortical cytoskeleton in the regulation of S-EPCS dynamics and ER-PM connectivity, and we identify the accumulation of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] at the PM as a molecular signal associated with the ER-PM connectivity changes. Our study highlights the functional conservation of EPCS components and PM phosphoinositides as modulators of ER-PM connectivity in eukaryotes, and uncovers unique aspects of the spatiotemporal regulation of ER-PM connectivity in plants.


Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Cell Membrane/metabolism , Endoplasmic Reticulum/metabolism , Phosphatidylinositols/metabolism , Stress, Physiological/physiology , Synaptotagmin I/metabolism , Cytoskeleton/metabolism , Eukaryota/metabolism , Phosphatidylinositol 4,5-Diphosphate/metabolism
9.
Curr Opin Plant Biol ; 40: 89-96, 2017 12.
Article En | MEDLINE | ID: mdl-28865976

The plant endoplasmic reticulum (ER) defines the biosynthetic site of lipids and proteins destined for secretion, but also contains important signal transduction and homeostasis components that regulate multiple hormonal and developmental responses. To achieve its various functions, the ER has a unique architecture, both reticulated and highly plastic, that facilitates the spatial-temporal segregation of biochemical reactions and the establishment of inter-organelle communication networks. At the cell cortex, the cortical ER (cER) anchors to and functionally couples with the PM through largely static structures known as ER-PM contact sites (EPCS). These spatially confined microdomains are emerging as critical regulators of the geometry of the cER network, and as highly specialized signalling hubs. In this review, we share recent insights into how EPCS regulate cER remodelling, and discuss the proposed roles for plant EPCS components in the integration of environmental and developmental signals at the cER-PM interface.


Cell Membrane/microbiology , Endoplasmic Reticulum/metabolism , Organelle Biogenesis , Plant Physiological Phenomena , Signal Transduction , Cell Membrane/metabolism
10.
Plant Cell Physiol ; 58(3): 478-484, 2017 03 01.
Article En | MEDLINE | ID: mdl-28100648

Membrane contact sites are recognized across eukaryotic systems as important nanostructures. Endoplasmic reticulum (ER)-plasma membrane (PM) contact sites (EPCS) are involved in excitation-contraction coupling, signaling, and plant responses to stress. In this report, we perform a multiscale structural analysis of Arabidopsis EPCS that combines live cell imaging, quantitative transmission electron microscopy (TEM) and electron tomography over a developmental gradient. To place EPCS in the context of the entire cortical ER, we examined green fluorescent protein (GFP)-HDEL in living cells over a developmental gradient, then Synaptotagmin1 (SYT1)-GFP was used as a specific marker of EPCS. In all tissues examined, young, rapidly elongating cells showed lamellar cortical ER and higher density of SYT1-GFP puncta, while in mature cells the cortical ER network was tubular, highly dynamic and had fewer SYT1-labeled puncta. The higher density of EPCS in young cells was verified by quantitative TEM of cryo-fixed tissues. For all cell types, the size of each EPCS had a consistent range in length along the PM from 50 to 300 nm, with microtubules and ribosomes excluded from the EPCS. The structural characterization of EPCS in different plant tissues, and the correlation of EPCS densities over developmental gradients illustrate how ER-PM communication evolves in response to cellular expansion.


Cell Membrane/metabolism , Cell Membrane/ultrastructure , Endoplasmic Reticulum/metabolism , Endoplasmic Reticulum/ultrastructure , Arabidopsis/metabolism , Arabidopsis/ultrastructure , Green Fluorescent Proteins/metabolism , Green Fluorescent Proteins/ultrastructure , Microscopy, Electron, Transmission , Microtubules/metabolism , Microtubules/ultrastructure , Ribosomes/metabolism , Ribosomes/ultrastructure
11.
Trends Cell Biol ; 26(9): 705-717, 2016 09.
Article En | MEDLINE | ID: mdl-27318776

The coordination of multiple metabolic activities in plants relies on an interorganelle communication network established through membrane contact sites (MCS). The MCS are maintained in transient or durable configurations by tethering structures which keep the two membranes in close proximity, and create chemical microdomains that allow localized and targeted exchange of small molecules and possibly proteins. The past few years have witnessed a dramatic increase in our understanding of the structural and molecular organization of plant interorganelle MCS, and their crucial roles in plant specialized functions including stress responses, cell to cell communication, and lipid transport. In this review we summarize recent advances in understanding the molecular components, structural organization, and functions of different plant-specific MCS architectures.


Cell Membrane/metabolism , Organelles/metabolism , Plants/metabolism , Biological Evolution , Eukaryotic Cells/metabolism , Lipids/chemistry
12.
Annu Rev Plant Biol ; 67: 337-64, 2016 04 29.
Article En | MEDLINE | ID: mdl-26905652

Multicellularity differs in plants and animals in that the cytoplasm, plasma membrane, and endomembrane of plants are connected between cells through plasmodesmal pores. Plasmodesmata (PDs) are essential for plant life and serve as conduits for the transport of proteins, small RNAs, hormones, and metabolites during developmental and defense signaling. They are also the only pathways available for viruses to spread within plant hosts. The membrane organization of PDs is unique, characterized by the close apposition of the endoplasmic reticulum and the plasma membrane and spoke-like filamentous structures linking the two membranes, which define PDs as membrane contact sites (MCSs). This specialized membrane arrangement is likely critical for PD function. Here, we review how PDs govern developmental and defensive signaling in plants, compare them with other types of MCSs, and discuss in detail the potential functional significance of the MCS nature of PDs.


Cell Membrane , Cytoskeleton , Endoplasmic Reticulum , Plant Cells/physiology , Plants , Plasmodesmata/physiology , Animals , Biological Transport , Signal Transduction
13.
Methods Mol Biol ; 1363: 175-87, 2016.
Article En | MEDLINE | ID: mdl-26577789

C2 domains (C2s) are regulatory protein modules identified in eukaryotic proteins targeted to cell membranes. C2s were initially characterized as independently folded Ca(2+)-dependent phospholipids binding domains; however, later studies have shown that C2s have evolutionarily diverged into Ca(2+)-dependent and Ca(2+)-independent forms. These forms interact and regulate their affinity to diverse lipid species using different binding mechanisms. In this protocol we describe a biochemical approach to produce, purify, and solubilize functional C2 domains bound to GST for the identification of their putative Ca(2+)-dependent and Ca(2+)-independent lipid-binding partners.


Membrane Lipids/metabolism , Protein Interaction Domains and Motifs , Proteins/metabolism , Calcium/metabolism , Phospholipids/metabolism , Protein Binding , Proteins/chemistry , Proteins/genetics , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/isolation & purification , Recombinant Fusion Proteins/metabolism
14.
Plant Physiol ; 168(1): 132-43, 2015 May.
Article En | MEDLINE | ID: mdl-25792253

Eukaryotic endoplasmic reticulum (ER)-plasma membrane (PM) contact sites are evolutionarily conserved microdomains that have important roles in specialized metabolic functions such as ER-PM communication, lipid homeostasis, and Ca(2+) influx. Despite recent advances in knowledge about ER-PM contact site components and functions in yeast (Saccharomyces cerevisiae) and mammals, relatively little is known about the functional significance of these structures in plants. In this report, we characterize the Arabidopsis (Arabidopsis thaliana) phospholipid binding Synaptotagmin1 (SYT1) as a plant ortholog of the mammal extended synaptotagmins and yeast tricalbins families of ER-PM anchors. We propose that SYT1 functions at ER-PM contact sites because it displays a dual ER-PM localization, it is enriched in microtubule-depleted regions at the cell cortex, and it colocalizes with Vesicle-Associated Protein27-1, a known ER-PM marker. Furthermore, biochemical and physiological analyses indicate that SYT1 might function as an electrostatic phospholipid anchor conferring mechanical stability in plant cells. Together, the subcellular localization and functional characterization of SYT1 highlights a putative role of plant ER-PM contact site components in the cellular adaptation to environmental stresses.


Adaptation, Physiological , Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Cell Membrane/metabolism , Endoplasmic Reticulum/metabolism , Stress, Mechanical , Synaptotagmin I/metabolism , Arabidopsis Proteins/chemistry , Cell Membrane/ultrastructure , Endoplasmic Reticulum/ultrastructure , Microtubules/metabolism , Models, Biological , Phosphatidylinositol Phosphates/metabolism , Protein Binding , Protein Structure, Tertiary , Protein Transport , Synaptotagmin I/chemistry
15.
Mol Plant ; 8(7): 1090-102, 2015 Jul.
Article En | MEDLINE | ID: mdl-25707755

The existence of multigenic families in the mevalonate pathway suggests divergent functional roles for pathway components involved in the biosynthesis of plant sterols. Squalene epoxidases (SQEs) are key components of this pathway, and Squalene Epoxidase 1 (SQE1) has been identified as a fundamental enzyme in this biosynthetic step. In the present work, we extended the characterization of the remaining SQE family members, phylogenetically resolving between true SQEs and a subfamily of SQE-like proteins that is exclusive to Brassicaceae. Functional characterization of true SQE family members, Squalene Epoxidase 2 (SQE2) and Squalene Epoxidase 3 (SQE3), indicates that SQE3, but not SQE2, contributes to the bulk SQE activity in Arabidopsis, with sqe3-1 mutants accumulating squalene and displaying sensitivity to terbinafine. We genetically demonstrated that SQE3 seems to play a particularly significant role in embryo development. Also, SQE1 and SQE3 both localize in the endoplasmic reticulum, and SQE3 can functionally complement SQE1. Thus, SQE1 and SQE3 seem to be two functionally unequal redundant genes in the promotion of plant SQE activity in Arabidopsis.


Arabidopsis/enzymology , Arabidopsis/growth & development , Seeds/enzymology , Seeds/growth & development , Squalene Monooxygenase/genetics , Squalene Monooxygenase/metabolism , Arabidopsis/cytology , Arabidopsis/genetics , Endoplasmic Reticulum/metabolism , Gene Expression Regulation, Plant , Genetic Complementation Test , Mutation , Phylogeny , Protein Transport , Seeds/cytology , Seeds/genetics
16.
Front Plant Sci ; 5: 709, 2014.
Article En | MEDLINE | ID: mdl-25566283

Plant adaptation, growth and development rely on the integration of many environmental and endogenous signals that collectively determine the overall plant phenotypic plasticity. Plant signaling molecules, also known as phytohormones, are fundamental to this process. These molecules act at low concentrations and regulate multiple aspects of plant fitness and development via complex signaling networks. By its nature, phytohormone research lies at the interface between chemistry and biology. Classically, the scientific community has always used synthetic phytohormones and analogs to study hormone functions and responses. However, recent advances in synthetic and combinational chemistry, have allowed a new field, plant chemical biology, to emerge and this has provided a powerful tool with which to study phytohormone function. Plant chemical biology is helping to address some of the most enduring questions in phytohormone research such as: Are there still undiscovered plant hormones? How can we identify novel signaling molecules? How can plants activate specific hormone responses in a tissue-specific manner? How can we modulate hormone responses in one developmental context without inducing detrimental effects on other processes? The chemical genomics approaches rely on the identification of small molecules modulating different biological processes and have recently identified active forms of plant hormones and molecules regulating many aspects of hormone synthesis, transport and response. We envision that the field of chemical genomics will continue to provide novel molecules able to elucidate specific aspects of hormone-mediated mechanisms. In addition, compounds blocking specific responses could uncover how complex biological responses are regulated. As we gain information about such compounds we can design small alterations to the chemical structure to further alter specificity, enhance affinity or modulate the activity of these compounds.

17.
Plant Cell ; 25(2): 728-43, 2013 Feb.
Article En | MEDLINE | ID: mdl-23404890

The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) enzyme catalyzes the major rate-limiting step of the mevalonic acid (MVA) pathway from which sterols and other isoprenoids are synthesized. In contrast with our extensive knowledge of the regulation of HMGR in yeast and animals, little is known about this process in plants. To identify regulatory components of the MVA pathway in plants, we performed a genetic screen for second-site suppressor mutations of the Arabidopsis thaliana highly drought-sensitive drought hypersensitive2 (dry2) mutant that shows decreased squalene epoxidase activity. We show that mutations in SUPPRESSOR OF DRY2 DEFECTS1 (SUD1) gene recover most developmental defects in dry2 through changes in HMGR activity. SUD1 encodes a putative E3 ubiquitin ligase that shows sequence and structural similarity to yeast Degradation of α factor (Doα10) and human TEB4, components of the endoplasmic reticulum-associated degradation C (ERAD-C) pathway. While in yeast and animals, the alternative ERAD-L/ERAD-M pathway regulates HMGR activity by controlling protein stability, SUD1 regulates HMGR activity without apparent changes in protein content. These results highlight similarities, as well as important mechanistic differences, among the components involved in HMGR regulation in plants, yeast, and animals.


Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Hydroxymethylglutaryl CoA Reductases/metabolism , Ubiquitin-Protein Ligases/metabolism , Arabidopsis/genetics , Arabidopsis Proteins/genetics , Humans , Membrane Proteins/genetics , Mevalonic Acid/metabolism , Mutation , Phenotype , Plant Roots/genetics , Plant Roots/growth & development , Plant Roots/metabolism , Plant Shoots/genetics , Plant Shoots/metabolism , Plants, Genetically Modified , Saccharomyces cerevisiae Proteins/genetics , Sequence Homology, Amino Acid , Sterols/metabolism , Ubiquitin-Protein Ligases/genetics
18.
Proc Natl Acad Sci U S A ; 109(48): 19537-44, 2012 Nov 27.
Article En | MEDLINE | ID: mdl-23144218

Upstream ORFs are elements found in the 5'-leader sequences of specific mRNAs that modulate the translation of downstream ORFs encoding major gene products. In Arabidopsis, the translational control of auxin response factors (ARFs) by upstream ORFs has been proposed as a regulatory mechanism required to respond properly to complex auxin-signaling inputs. In this study, we identify and characterize the aberrant auxin responses in specific ribosomal protein mutants in which multiple ARF transcription factors are simultaneously repressed at the translational level. This characteristic lends itself to the use of these mutants as genetic tools to bypass the genetic redundancy among members of the ARF family in Arabidopsis. Using this approach, we were able to assign unique functions for ARF2, ARF3, and ARF6 in plant development.


Arabidopsis Proteins/physiology , Gene Expression Regulation, Plant/physiology , Indoleacetic Acids/metabolism , Protein Biosynthesis/physiology , Ribosomal Proteins/physiology , Open Reading Frames , Protein Transport , Signal Transduction , Vacuoles/metabolism
19.
BMC Genomics ; 13: 187, 2012 May 14.
Article En | MEDLINE | ID: mdl-22583865

BACKGROUND: L-ascorbic acid (AsA; vitamin C) is essential for all living plants where it functions as the main hydrosoluble antioxidant. It has diverse roles in the regulation of plant cell growth and expansion, photosynthesis, and hormone-regulated processes. AsA is also an essential component of the human diet, being tomato fruit one of the main sources of this vitamin. To identify genes responsible for AsA content in tomato fruit, transcriptomic studies followed by clustering analysis were applied to two groups of fruits with contrasting AsA content. These fruits were identified after AsA profiling of an F8 Recombinant Inbred Line (RIL) population generated from a cross between the domesticated species Solanum lycopersicum and the wild relative Solanum pimpinellifollium. RESULTS: We found large variability in AsA content within the RIL population with individual RILs with up to 4-fold difference in AsA content. Transcriptomic analysis identified genes whose expression correlated either positively (PVC genes) or negatively (NVC genes) with the AsA content of the fruits. Cluster analysis using SOTA allowed the identification of subsets of co-regulated genes mainly involved in hormones signaling, such as ethylene, ABA, gibberellin and auxin, rather than any of the known AsA biosynthetic genes. Data mining of the corresponding PVC and NVC orthologs in Arabidopis databases identified flagellin and other ROS-producing processes as cues resulting in differential regulation of a high percentage of the genes from both groups of co-regulated genes; more specifically, 26.6% of the orthologous PVC genes, and 15.5% of the orthologous NVC genes were induced and repressed, respectively, under flagellin22 treatment in Arabidopsis thaliana. CONCLUSION: Results here reported indicate that the content of AsA in red tomato fruit from our selected RILs are not correlated with the expression of genes involved in its biosynthesis. On the contrary, the data presented here supports that AsA content in tomato fruit co-regulates with genes involved in hormone signaling and they are dependent on the oxidative status of the fruit.


Ascorbic Acid/metabolism , Fruit/metabolism , Genes, Plant/physiology , Solanum/metabolism , Cluster Analysis , Gene Expression Regulation, Plant/genetics , Gene Expression Regulation, Plant/physiology , Genes, Plant/genetics , Solanum lycopersicum/genetics , Solanum lycopersicum/metabolism , Oxidation-Reduction , Solanum/genetics
20.
Plant Physiol ; 158(3): 1252-66, 2012 Mar.
Article En | MEDLINE | ID: mdl-22232384

TETRATRICOPEPTIDE THIOREDOXIN-LIKE (TTL) proteins are characterized by the presence of six tetratricopeptide repeats in conserved positions and a carboxyl-terminal region known as the thioredoxin-like domain with homology to thioredoxins. In Arabidopsis (Arabidopsis thaliana), the TTL gene family is composed by four members, and the founder member, TTL1, is required for osmotic stress tolerance. Analysis of sequenced genomes indicates that TTL genes are specific to land plants. In this study, we report the expression profiles of Arabidopsis TTL genes using data mining and promoter-reporter ß-glucuronidase fusions. Our results show that TTL1, TTL3, and TTL4 display ubiquitous expression in normal growing conditions but differential expression patterns in response to osmotic and NaCl stresses. TTL2 shows a very different expression pattern, being specific to pollen grains. Consistent with the expression data, ttl1, ttl3, and ttl4 mutants show reduced root growth under osmotic stress, and the analysis of double and triple mutants indicates that TTL1, TTL3, and TTL4 have partially overlapping yet specific functions in abiotic stress tolerance while TTL2 is involved in male gametophytic transmission.


Adaptation, Physiological , Arabidopsis Proteins/metabolism , Arabidopsis/genetics , Stress, Physiological , Arabidopsis/drug effects , Arabidopsis/metabolism , Arabidopsis/physiology , Arabidopsis Proteins/classification , Arabidopsis Proteins/genetics , Computational Biology , Data Mining , Gene Expression Profiling , Gene Expression Regulation, Plant , Genes, Plant , Genes, Reporter , Glucuronidase/genetics , Glucuronidase/metabolism , Multigene Family , Mutation , Phylogeny , Plant Roots/genetics , Plant Roots/metabolism , Plant Roots/physiology , Plants, Genetically Modified/drug effects , Plants, Genetically Modified/genetics , Plants, Genetically Modified/metabolism , Plants, Genetically Modified/physiology , Pollen/genetics , Pollen/metabolism , Pollen/physiology , Promoter Regions, Genetic , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sodium Chloride/pharmacology
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