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TheScientificWorldJournal 2015WRKY proteins are emerging players in plant signaling and have been thoroughly reported to play important roles in plants under biotic stress like pathogen attack.... (Review)
Review
WRKY proteins are emerging players in plant signaling and have been thoroughly reported to play important roles in plants under biotic stress like pathogen attack. However, recent advances in this field do reveal the enormous significance of these proteins in eliciting responses induced by abiotic stresses. WRKY proteins act as major transcription factors, either as positive or negative regulators. Specific WRKY factors which help in the expression of a cluster of stress-responsive genes are being targeted and genetically modified to induce improved abiotic stress tolerance in plants. The knowledge regarding the signaling cascade leading to the activation of the WRKY proteins, their interaction with other proteins of the signaling pathway, and the downstream genes activated by them are altogether vital for justified targeting of the WRKY genes. WRKY proteins have also been considered to generate tolerance against multiple abiotic stresses with possible roles in mediating a cross talk between abiotic and biotic stress responses. In this review, we have reckoned the diverse signaling pattern and biological functions of WRKY proteins throughout the plant kingdom along with the growing prospects in this field of research.
Topics: Arabidopsis Proteins; Gene Expression Profiling; Gene Expression Regulation, Plant; Plant Proteins; Plants; Signal Transduction; Stress, Physiological
PubMed: 25879071
DOI: 10.1155/2015/807560 -
Developmental Cell Apr 2008About 200 plant biologists convened in Keystone, Colorado, for the "Plant Hormones and Signaling" symposium, which was organized by Joanne Chory, Joe Ecker, and Mark... (Review)
Review
About 200 plant biologists convened in Keystone, Colorado, for the "Plant Hormones and Signaling" symposium, which was organized by Joanne Chory, Joe Ecker, and Mark Estelle. The meeting was run concurrently with the "Plant Innate Immunity" symposium organized by Jonathan Jones and Jane Glazebrook. In this report, we summarize the progress in plant hormones and signaling.
Topics: Cell Nucleus; Congresses as Topic; Gene Expression Regulation, Plant; Molecular Structure; Plant Growth Regulators; Plant Physiological Phenomena; Plant Proteins; Signal Transduction; Transcription Factors
PubMed: 18410724
DOI: 10.1016/j.devcel.2008.03.013 -
Frontiers in Bioscience (Landmark... Dec 2021Abiotic stresses are wide-ranging environmental factors that adversely affect the yield and quality of tea plants (Camellia sinensis). As perennial woody economic... (Review)
Review
Abiotic stresses are wide-ranging environmental factors that adversely affect the yield and quality of tea plants (Camellia sinensis). As perennial woody economic plants, various environmental factors affect its growth and development. To survive under stress conditions, plants adapt to or withstand these adverse external environments by regulating their growth and morphological structure. Recently, there have been knowledges regarding the significant progress in the mechanisms of abiotic stresses (including cold and heat, drought, salt and heavy metal stresses) tolerance in tea plants. Many evidences suggest that several phytohormones are in response to various environmental stresses, and regulate plant stress adaptation. However, the regulatory mechanisms of plant abiotic stress responses and resistance remain unclear. In this review, we mainly summarize the studies on the adaptive physiological and molecular mechanisms of tea plants under abiotic stress, and discuss the direction for tea plant resistance and breeding strategies.
Topics: Adaptation, Physiological; Camellia sinensis; Gene Expression Regulation, Plant; Plant Proteins; Stress, Physiological
PubMed: 34994184
DOI: 10.52586/5063 -
Planta Nov 2016The non-specific lipid transfer proteins (LTPs) constitute a large protein family found in all land plants. They are small proteins characterized by a tunnel-like... (Review)
Review
The non-specific lipid transfer proteins (LTPs) constitute a large protein family found in all land plants. They are small proteins characterized by a tunnel-like hydrophobic cavity, which makes them suitable for binding and transporting various lipids. The LTPs are abundantly expressed in most tissues. In general, they are synthesized with an N-terminal signal peptide that localizes the protein to spaces exterior to the plasma membrane. The in vivo functions of LTPs are still disputed, although evidence has accumulated for a role in the synthesis of lipid barrier polymers, such as cuticular waxes, suberin, and sporopollenin. There are also reports suggesting that LTPs are involved in signaling during pathogen attacks. LTPs are considered as key proteins for the plant's survival and colonization of land. In this review, we aim to present an overview of the current status of LTP research and also to discuss potential future applications of these proteins. We update the knowledge on 3D structures and lipid binding and review the most recent data from functional investigations, such as from knockout or overexpressing experiments. We also propose and argument for a novel system for the classification and naming of the LTPs.
Topics: Carrier Proteins; Ligands; Plant Proteins; Plants; Terminology as Topic
PubMed: 27562524
DOI: 10.1007/s00425-016-2585-4 -
Cellular & Molecular Biology Letters Mar 2011Plants are attacked by a wide spectrum of pathogens, being the targets of viruses, bacteria, fungi, protozoa, nematodes and insects. Over the course of their evolution,... (Review)
Review
Plants are attacked by a wide spectrum of pathogens, being the targets of viruses, bacteria, fungi, protozoa, nematodes and insects. Over the course of their evolution, plants have developed numerous defense mechanisms including the chemical and physical barriers that are constitutive elements of plant cell responses locally and/or systemically. However, the modern approach in plant sciences focuses on the evolution and role of plant protein receptors corresponding to specific pathogen effectors. The recognition of an invader's molecules could be in most cases a prerequisite sine qua non for plant survival. Although the predicted three-dimensional structure of plant resistance proteins (R) is based on research on their animal homologs, advanced technologies in molecular biology and bioinformatics tools enable the investigation or prediction of interaction mechanisms for specific receptors with pathogen effectors. Most of the identified R proteins belong to the NBS-LRR family. The presence of other domains (including the TIR domain) apart from NBS and LRR is fundamental for the classification of R proteins into subclasses. Recently discovered additional domains (e.g. WRKY) of R proteins allowed the examination of their localization in plant cells and the role they play in signal transduction during the plant resistance response to biotic stress factors. This review focuses on the current state of knowledge about the NBS-LRR family of plant R proteins: their structure, function and evolution, and the role they play in plant innate immunity.
Topics: Evolution, Molecular; Immunity, Innate; Models, Molecular; Plant Proteins; Plants; Protein Structure, Tertiary; Signal Transduction
PubMed: 20585889
DOI: 10.2478/s11658-010-0024-2 -
The Plant Cell Dec 2010Both transcriptional (TGS) and posttranscriptional gene silencing (PTGS) are conserved eukaryotic gene regulatory mechanisms, integral for taming exogenous (viruses and... (Review)
Review
Both transcriptional (TGS) and posttranscriptional gene silencing (PTGS) are conserved eukaryotic gene regulatory mechanisms, integral for taming exogenous (viruses and bacteria) or endogenous (repetitive elements and transposons) invasive nucleic acids to minimize their impact on genome integrity and function. TGS and PTGS also are essential for controlling the expression of protein coding genes throughout development or in response to environmental stimuli. In plants and animals, at least one member of the conserved ARGONAUTE (AGO) protein family comprises the catalytic engine of the silencing complex, which is guided by sequence-specific small RNA to cognate RNA. In this review, we present general features of plant and animal AGO proteins and detail our knowledge on the 10 Arabidopsis thaliana AGOs.
Topics: Biocatalysis; Gene Expression Regulation, Plant; Genes, Plant; Plant Proteins; Protein Binding; Protein Processing, Post-Translational; RNA Processing, Post-Transcriptional
PubMed: 21183704
DOI: 10.1105/tpc.110.080671 -
The FEBS Journal Aug 2008Over the years, several studies have been performed to analyse plant-pathogen interactions. Recently, functional genomic strategies, including proteomics and... (Review)
Review
Over the years, several studies have been performed to analyse plant-pathogen interactions. Recently, functional genomic strategies, including proteomics and transcriptomics, have contributed to the effort of defining gene and protein function and expression profiles. Using these 'omic' approaches, pathogenicity- and defence-related genes and proteins expressed during phytopathogen infections have been identified and enormous datasets have been accumulated. However, the understanding of molecular plant-pathogen interactions is still an intriguing area of investigation. Proteomics has dramatically evolved in the pursuit of large-scale functional assignment of candidate proteins and, by using this approach, several proteins expressed during phytopathogenic interactions have been identified. In this review, we highlight the proteins expressed during plant-virus, plant-bacterium, plant-fungus and plant-nematode interactions reported in proteomic studies, and discuss these findings considering the advantages and limitations of current proteomic tools.
Topics: Animals; Nematoda; Plant Proteins; Plants; Proteomics
PubMed: 18616468
DOI: 10.1111/j.1742-4658.2008.06528.x -
Nature Immunology Dec 2006Plant proteins belonging to the nucleotide-binding site-leucine-rich repeat (NBS-LRR) family are used for pathogen detection. Like the mammalian Nod-LRR protein... (Review)
Review
Plant proteins belonging to the nucleotide-binding site-leucine-rich repeat (NBS-LRR) family are used for pathogen detection. Like the mammalian Nod-LRR protein 'sensors' that detect intracellular conserved pathogen-associated molecular patterns, plant NBS-LRR proteins detect pathogen-associated proteins, most often the effector molecules of pathogens responsible for virulence. Many virulence proteins are detected indirectly by plant NBS-LRR proteins from modifications the virulence proteins inflict on host target proteins. However, some NBS-LRR proteins directly bind pathogen proteins. Association with either a modified host protein or a pathogen protein leads to conformational changes in the amino-terminal and LRR domains of plant NBS-LRR proteins. Such conformational alterations are thought to promote the exchange of ADP for ATP by the NBS domain, which activates 'downstream' signaling, by an unknown mechanism, leading to pathogen resistance.
Topics: Amino Acid Sequence; Animals; Leucine-Rich Repeat Proteins; Molecular Sequence Data; Plant Proteins; Plants; Protein Structure, Tertiary; Proteins; Sequence Homology, Amino Acid
PubMed: 17110940
DOI: 10.1038/ni1410 -
FEBS Letters Feb 2018The plant-specific GAI-RGA-and-SCR (GRAS) family of proteins function as transcriptional regulators and play critical roles in development and signalling. Recent... (Review)
Review
The plant-specific GAI-RGA-and-SCR (GRAS) family of proteins function as transcriptional regulators and play critical roles in development and signalling. Recent structural studies have shed light on the molecular functions at the structural level. The conserved GRAS domain comprises an α-helical cap and α/β core subdomains. The α-helical cap mediates head-to-head heterodimerization between SHR and SCR GRAS domains. This type of dimerization is predicted for the NSP1-NSP2 heterodimer and DELLA proteins such as RGA and SLR1 homodimers. The α/β core subdomain possesses a hydrophobic groove formed by surface α3- and α7-helices and mediates protein-protein interactions. The groove of the SHR GRAS domain accommodates the zinc fingers of JKD, a BIRD/IDD family transcription factor, while the groove of the SCL7 GRAS domain mediates the SCL7 homodimerization.
Topics: Plant Proteins; Protein Binding; Protein Domains; Protein Multimerization; Protein Structure, Quaternary; Substrate Specificity
PubMed: 29364510
DOI: 10.1002/1873-3468.12987 -
International Journal of Molecular... Mar 2020Intrinsically disordered proteins and regions typically lack a well-defined structure and thus fall outside the scope of the classic sequence-structure-function... (Review)
Review
Intrinsically disordered proteins and regions typically lack a well-defined structure and thus fall outside the scope of the classic sequence-structure-function relationship. Hence, classic sequence- or structure-based bioinformatic approaches are often not well suited to identify homology or predict the function of unknown intrinsically disordered proteins. Here, we give selected examples of intrinsic disorder in plant proteins and present how protein function is shared, altered or distinct in evolutionary distant organisms. Furthermore, we explore how examining the specific role of disorder across different phyla can provide a better understanding of the common features that protein disorder contributes to the respective biological mechanism.
Topics: Animals; Evolution, Molecular; Gene Expression Regulation; Humans; Intrinsically Disordered Proteins; Plant Proteins; Plants; Protein Conformation; Protein Folding
PubMed: 32204351
DOI: 10.3390/ijms21062105