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Current Opinion in Plant Biology Aug 1999Plant disease resistance (R) genes encode proteins that both determine recognition of specific pathogen-derived avirulence (Avr) proteins and initiate signal... (Review)
Review
Plant disease resistance (R) genes encode proteins that both determine recognition of specific pathogen-derived avirulence (Avr) proteins and initiate signal transduction pathways leading to complex defense responses. Recent developments suggest that recognition specificity of R proteins is determined by either a protein kinase domain or by a region consisting of leucine-rich repeats. R genes conferring resistance to bacterial, viral, and fungal pathogens appear to use multiple signaling pathways, some of which involve distinct proteins and others which converge upon common downstream effectors. Manipulation of R genes and their signaling pathways by transgenic expression is a promising strategy to improve disease resistance in plants.
Topics: Calcium-Calmodulin-Dependent Protein Kinases; Genes, Plant; Plant Diseases; Plant Proteins; Signal Transduction
PubMed: 10458999
DOI: 10.1016/S1369-5266(99)80049-1 -
Biophysical Journal Jun 2011Aureochrome is a recently discovered blue light photosensor that controls a light-dependent morphology change. As a photosensor, it has a unique DNA binding domain...
Aureochrome is a recently discovered blue light photosensor that controls a light-dependent morphology change. As a photosensor, it has a unique DNA binding domain (bZIP). Although the biological functions of aureochrome have been revealed, the fundamental photochemistry of this protein has not been elucidated. The photochemical reaction dynamics of the LOV (light, oxygen, or voltage) domain of aureochrome-1 (AUREO1-LOV) and the LOV domain with the bZIP domain (AUREO1-ZL) were studied by employing the transient-grating (TG) technique, using size-exclusion chromatography to verify results. For both samples, adduct formation takes place with a time constant of 2.8 μs. Although significant diffusion changes were observed for both AUREO1-LOV and AUREO1-ZL after adduct formation, the origins of these changes were significantly different. The TG signal of AUREO1-LOV was strongly concentration-dependent. From analysis of the signal, it was concluded that AUREO1-LOV exists in equilibrium between the monomer and dimer, and dimerization of the monomer is the main reaction, i.e., irradiation with blue light enhances the strength of the interdomain interaction. On the other hand, the reaction of AUREO1-ZL is independent of concentration, suggesting that an intraprotein conformational change occurs in the bZIP domain with a time constant of 160 ms. These results revealed the different reactions and roles of the two domains; the LOV domain acts as a photosensor, leading to a subsequent conformational change in the bZIP domain, which should change its ability to bind to DNA. A model is proposed that demonstrates how aureochrome uses blue light to control its affinity for DNA.
Topics: Amino Acid Sequence; Chlorophyta; Chromatography, Gel; Diffusion; Kinetics; Lasers; Light; Photochemical Processes; Plant Proteins; Protein Structure, Tertiary
PubMed: 21641326
DOI: 10.1016/j.bpj.2011.02.043 -
Journal of Experimental Botany 2009A highly evolved surveillance system in plants is able to detect a broad range of signals originating from pathogens, damaged tissues, or altered developmental... (Review)
Review
A highly evolved surveillance system in plants is able to detect a broad range of signals originating from pathogens, damaged tissues, or altered developmental processes, initiating sophisticated molecular mechanisms that result in defence, wound healing, and development. Microbe-associated molecular pattern molecules (MAMPs), damage-associated molecular pattern molecules (DAMPs), virulence factors, secreted proteins, and processed peptides can be recognized directly or indirectly by this surveillance system. Nucleotide binding-leucine rich repeat proteins (NB-LRR) are intracellular receptors and have been targeted by breeders for decades to elicit resistance to crop pathogens in the field. Receptor-like kinases (RLKs) or receptor like proteins (RLPs) are membrane bound signalling molecules with an extracellular receptor domain. They provide an early warning system for the presence of potential pathogens and activate protective immune signalling in plants. In addition, they act as a signal amplifier in the case of tissue damage, establishing symbiotic relationships and effecting developmental processes. The identification of several important ligands for the RLK-type receptors provided an opportunity to understand how plants differentiate, how they distinguish beneficial and detrimental stimuli, and how they co-ordinate the role of various types of receptors under varying environmental conditions. The diverse roles of extra-and intracellular plant receptors are examined here and the recent findings on how they promote defence and development is reviewed.
Topics: Plant Proteins; Plants; Receptors, Cell Surface; Signal Transduction
PubMed: 19628572
DOI: 10.1093/jxb/erp233 -
Current Opinion in Plant Biology Aug 2023To successfully colonise plants, pathogens must circumvent the plant immune system. Intracellular immune receptors of the nucleotide-binding leucine-rich repeat (NLR)... (Review)
Review
To successfully colonise plants, pathogens must circumvent the plant immune system. Intracellular immune receptors of the nucleotide-binding leucine-rich repeat (NLR) class of proteins are major components of the plant immune system. NLRs function as disease resistance genes by recognising effectors secreted by diverse pathogens, triggering a localised form of programmed cell death known as the hypersensitive response. To evade detection, effectors have evolved to suppress NLR-mediated immunity by targeting NLRs either directly or indirectly. Here, we compile the latest discoveries related to NLR-suppressing effectors and categorise these effectors based on their mode of action. We discuss the diverse strategies pathogens use to perturb NLR-mediated immunity, and how we can use our understanding of effector activity to help guide new approaches for disease resistance breeding.
Topics: Disease Resistance; Plant Breeding; Plants; Plant Immunity; Plant Diseases; Plant Proteins
PubMed: 37295294
DOI: 10.1016/j.pbi.2023.102396 -
Journal of Experimental Botany Aug 2016
Topics: Peptides; Plant Proteins; Plants; Signal Transduction
PubMed: 27521600
DOI: 10.1093/jxb/erw309 -
Cell Stress & Chaperones Dec 1996Based on the partial or complete sequences of 14 plant heat stress transcription factors (Hsfs) from tomato, soybean, Arabidopsis and maize we propose a general... (Review)
Review
Based on the partial or complete sequences of 14 plant heat stress transcription factors (Hsfs) from tomato, soybean, Arabidopsis and maize we propose a general nomenclature with two basic classes, i.e. classes A and B each containing two or more types of Hsfs (HsfA1, HsfA2 etc.). Despite some plant-specific peculiarities, essential functional domains and modules of these proteins are conserved among plants, yeast, Drosophila and vertebrates. A revised terminology of these parts follows recommendations agreed upon among the authors and representatives from other laboratories working in this field (see legend to Fig. 1). Similar to the situation with the small heat shock proteins (sHsps), the complexity of the hsf gene family in plants appears to be higher than in other eukaryotic organisms.
Topics: Amino Acid Sequence; Animals; Heat-Shock Proteins; Humans; Molecular Sequence Data; Plant Proteins; Transcription Factors
PubMed: 9222607
DOI: 10.1379/1466-1268(1996)001<0215:thwcap>2.3.co;2 -
Current Opinion in Plant Biology Oct 2007ROP/RAC GTPases are versatile signaling molecules in plants. Recent studies of ROP/RAC regulators and effectors have generated new insights into the molecular basis of... (Review)
Review
ROP/RAC GTPases are versatile signaling molecules in plants. Recent studies of ROP/RAC regulators and effectors have generated new insights into the molecular basis of their functional versatility. Significant progress has also been made in our understanding of the mechanism for the localization of ROP/RAC signaling to specific domains of the plasma membrane.
Topics: GTP Phosphohydrolases; Plant Proteins; Signal Transduction
PubMed: 17709276
DOI: 10.1016/j.pbi.2007.07.005 -
Plant Physiology Sep 2008
Review
Topics: Adaptation, Physiological; Molecular Structure; Plant Proteins; Plants; Water
PubMed: 18772351
DOI: 10.1104/pp.108.120725 -
Plant Signaling & Behavior Apr 2011To optimize photosynthetic activity, chloroplasts change their intracellular location in response to ambient light conditions; chloroplasts move toward low intensity... (Review)
Review
To optimize photosynthetic activity, chloroplasts change their intracellular location in response to ambient light conditions; chloroplasts move toward low intensity light to maximize light capture, and away from high intensity light to avoid photodamage. Although several proteins have been reported to be involved in the chloroplast photorelocation movement response, any physical interaction among them was not found so far. We recently found a physical interaction between two plant-specific coiled-coil proteins, WEB1 (Weak Chloroplast Movement under Blue Light 1) and PMI2 (Plastid Movement Impaired 2), that were identified to regulate chloroplast movement velocity. Since the both coiled-coil regions of WEB1 and PMI2 were classified into an uncharacterized protein family having DUF827 (DUF: Domain of Unknown Function) domain, it was the first report that DUF827 proteins could mediate protein-protein interaction. In this mini-review article, we discuss regarding molecular function of WEB1 and PMI2, and also define a novel protein family composed of WEB1, PMI2 and WEB1/PMI2-like proteins for protein-protein interaction in land plants.
Topics: Arabidopsis Proteins; Carrier Proteins; Chloroplasts; Plant Proteins; Protein Binding
PubMed: 21389774
DOI: 10.4161/psb.6.4.14784 -
The Plant Cell Jul 1995
Review
Topics: Albumins; Plant Proteins; Protein Conformation; Seeds
PubMed: 7640527
DOI: 10.1105/tpc.7.7.945