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Peptides Jun 2021Plant AMPs are usually cysteine-rich, and can be classified in several classes, including lipid transfer proteins (LTPs). LTPs are small plant cationic peptides, and can... (Review)
Review
Plant AMPs are usually cysteine-rich, and can be classified in several classes, including lipid transfer proteins (LTPs). LTPs are small plant cationic peptides, and can be classified in two subclasses, LTP (9-10 kDa) and LTP (7 kDa). They have been identified and isolated from various plant species and can be involved in a number of processes, including responses against several phytopathogens. LTP presents 4 parallel α- helices and a 3-helix fragment. These structures form a tunnel with large and small entrances. LTP presents 3 parallel α- helices, which form a cavity with triangular structure. Both LTP subclasses present a hydrophobic cavity, which makes interaction with different lipids and general hydrophobic molecules possible. Several studies report a broad spectrum of activity of plant LTPs, including antibacterial, antifungal, antiviral, antitumoral, and insecticidal activity. Thus, these molecules can be employed in human and animal health as an alternative to the conventional treatment of disease, well as providing the source of novel drugs. However, employing peptides in human health can present challenges, such as the toxicity of peptides, the difference between the results found in in vitro assays and in pre-clinical or clinical tests and their low efficiency against Gram-negative bacteria. In this context, plant LTPs can be an interesting alternative means by which to bypass such challenges. This review addresses the versatility of plant LTPs, their broad spectrum of activities and their potential applications in human and animal health and in agricultural production, and examines challenges in their biotechnological application.
Topics: Animals; Anti-Infective Agents; Antigens, Plant; Antineoplastic Agents; Biotechnology; Carrier Proteins; Humans; Models, Molecular; Plant Proteins; Protein Conformation
PubMed: 33746031
DOI: 10.1016/j.peptides.2021.170531 -
Current Opinion in Plant Biology Aug 2017Plant pathogens are a serious threat to agriculture and to global food security, causing diverse crop diseases which lead to extensive annual yield losses. Production of... (Review)
Review
Plant pathogens are a serious threat to agriculture and to global food security, causing diverse crop diseases which lead to extensive annual yield losses. Production of effector proteins by pathogens, to manipulate host cellular processes, is central to their success. An understanding of fundamental effector biology is key to addressing the threat posed by these pathogens. Recent advances in 'omics' technologies have facilitated high-throughput identification of putative effector proteins, while evolving cellular, structural and biochemical approaches have assisted in characterising their function. Furthermore, structures of effectors in complex with host factors now provide opportunities for applying our knowledge of effector biology to influence disease outcomes. In this review, we highlight recent advances in the field and suggest avenues for future research.
Topics: Agriculture; Host-Pathogen Interactions; Plant Diseases; Plant Proteins
PubMed: 28460241
DOI: 10.1016/j.pbi.2017.04.013 -
Plant Science : An International... Feb 2019When facing microbe invaders, plants activate genetic and metabolic defense mechanisms and undergo extracellular and intracellular changes to obtain a certain level of... (Review)
Review
When facing microbe invaders, plants activate genetic and metabolic defense mechanisms and undergo extracellular and intracellular changes to obtain a certain level of host resistance. Dynamic adjustment and adaptation occur in structures containing lipophilic compounds and cellular metabolites. Lipids encompassing fatty acids, fatty acid-based polymers, and fatty acid derivatives are part of the fundamental architecture of cells and tissues and are essential compounds in numerous biological processes. Lipid-associated plant defense responses are mostly facilitated by the activation of lipases (lipid hydrolyzing proteins), which cleave or transform lipid substrates in various subcellular compartments. In this review, several types of plant defense-associated lipases are described, including their molecular aspects, enzymatic actions, cellular functions, and possible functional relevance in plant defense. Defensive roles are discussed considering enzyme properties, lipid metabolism, downstream regulation, and phenotypic traits in loss-of-function mutants.
Topics: Host-Pathogen Interactions; Lipase; Lipid Metabolism; Plant Diseases; Plant Immunity; Plant Proteins
PubMed: 30709493
DOI: 10.1016/j.plantsci.2018.07.003 -
International Journal of Biological... Apr 2018An increasing use of vegetable protein is required to support the production of protein-rich foods which can replace animal proteins in the human diet. Amaranth, chia... (Review)
Review
An increasing use of vegetable protein is required to support the production of protein-rich foods which can replace animal proteins in the human diet. Amaranth, chia and quinoa seeds contain proteins which have biological and functional properties that provide nutritional benefits due to their reasonably well-balanced aminoacid content. This review analyses these vegetable proteins and focuses on recent research on protein classification and isolation as well as structural characterization by means of fluorescence spectroscopy, surface hydrophobicity and differential scanning calorimetry. Isolation procedures have a profound influence on the structural properties of the proteins and, therefore, on their in vitro digestibility. The present article provides a comprehensive overview of the properties and characterization of these proteins.
Topics: Amaranthus; Anthemis; Chemical Phenomena; Chenopodium quinoa; Molecular Structure; Plant Proteins; Seeds
PubMed: 29247732
DOI: 10.1016/j.ijbiomac.2017.12.080 -
Chembiochem : a European Journal of... Jan 2021Pathogenesis-related (PR) proteins constitute a broad class of plant proteins with analogues found throughout nature from bacteria to higher eukaryotes. PR proteins were... (Review)
Review
Pathogenesis-related (PR) proteins constitute a broad class of plant proteins with analogues found throughout nature from bacteria to higher eukaryotes. PR proteins were first noted in plants as part of the hypersensitive response, but have since been assigned an array of biological roles. The PR10/Bet v1-like proteins are a subset of PR proteins characterized by an ability to bind a wide range of lipophilic ligands, uniquely positioning them as contributors to specialized biosynthetic pathways. PR10/Bet v1-like proteins participate in the production of plant alkaloids and phenolics including flavonoids, both as general binding proteins and in special cases as catalysts. Owing initially to the perceived allergenic properties of PR10/Bet v1-like proteins, many were studied at the structural level to elucidate the basis for ligand binding. These studies provided a foundation for more recent efforts to understand higher-level structural order and how PR10/Bet v1-like proteins catalyse key reactions in plant pathways. Synthetic biology aimed at reconstituting plant-specialized metabolism in microorganisms uses knowledge of these proteins to fine-tune performance in new systems.
Topics: Allergens; Molecular Structure; Plant Proteins
PubMed: 32700448
DOI: 10.1002/cbic.202000354 -
Trends in Plant Science Nov 2016Flowering plants convert many hundreds of organelle cytidines (Cs) to uridines (Us) during post-transcriptional RNA editing. Pentatricopeptide repeat (PPR) proteins... (Review)
Review
Flowering plants convert many hundreds of organelle cytidines (Cs) to uridines (Us) during post-transcriptional RNA editing. Pentatricopeptide repeat (PPR) proteins dictate specificity by recognizing RNA sequences near C targets. However, the complete mechanism of the editing machinery is not yet understood. Recently, non-PPR editing factors [RNA editing factor interacting proteins (RIPs)/multiple organellar RNA editing factors (MORFs), organelle RNA recognition motif (ORRM) proteins, organelle zinc-finger (OZ) proteins, and protoporphyrinogen oxidase 1 (PPO1)] have been identified as components of the plant RNA editosome, which is a small RNA-protein complex. Surprisingly, plant editosomes are highly diverse not only with regard to the PPR proteins they contain but also in the non-PPR components that are present. Here we review the most recent progress in the field and discuss the implications of the diversity of plant editosomes for the evolution of RNA editing and for possible future applications.
Topics: Chloroplasts; Organelles; Plant Proteins; RNA Editing; RNA, Plant
PubMed: 27491516
DOI: 10.1016/j.tplants.2016.07.005 -
Trends in Plant Science Feb 2016LATERAL ORGAN BOUNDARIES DOMAIN (LBD) proteins defined by a conserved LATERAL ORGAN BOUNDARIES (LOB) domain are key regulators of plant organ development. Recent studies... (Review)
Review
LATERAL ORGAN BOUNDARIES DOMAIN (LBD) proteins defined by a conserved LATERAL ORGAN BOUNDARIES (LOB) domain are key regulators of plant organ development. Recent studies have expanded their functional diversity beyond the definition of lateral organ boundaries to pollen development, plant regeneration, photomorphogenesis, pathogen response, and specific developmental functions in non-model plants, such as poplar and legumes. The identification of a range of upstream regulators, protein partners, and downstream targets of LBD family members has unraveled the molecular networks of LBD-dependent processes. Moreover, it has been demonstrated that LBD proteins have essential roles in integrating developmental changes in response to phytohormone signaling or environmental cues. As we discuss here, these novel discoveries of LBD functions and their molecular contexts promote a better understanding of this plant-specific transcription factor family.
Topics: Organ Specificity; Plant Development; Plant Proteins; Protein Binding; Protein Structure, Tertiary
PubMed: 26616195
DOI: 10.1016/j.tplants.2015.10.010 -
Critical Reviews in Food Science and... 2023The development of novel protein sources to compensate for the expected future shortage of traditional animal proteins due to their high carbon footprint is a major... (Review)
Review
The development of novel protein sources to compensate for the expected future shortage of traditional animal proteins due to their high carbon footprint is a major contemporary challenge in the agri-food industry currently. Therefore, both industry and consumers are placing a greater emphasis on plant proteins as a sustainable source of protein to meet the growing nutritional demand of ever increasing population. In addition to being key alternatives, many plant-based foods have biological properties that make them potentially functional or health-promoting foods, particularly physiologically active peptides and proteins accounting for most of these properties. This review discusses the importance of plant-based protein as a viable and sustainable alternative to animal proteins. The current advances in plant protein isolation and production and characterization of bioactive hydrolysates and peptides from plant proteins are described comprehensively. Furthermore, the recent research on bioactivities and bioavailability of plant protein-derived bioactive peptides is reviewed briefly. The limitations of using bioactive peptides, regulatory criteria, and the possible future applications of plant protein-derived bioactive peptides are highlighted. This review may help understand plant proteins and their bioactive peptides and provide valuable suggestions for future research and applications in the food industry.
Topics: Peptides; Plant Proteins
PubMed: 35521961
DOI: 10.1080/10408398.2022.2067120 -
Plant Physiology and Biochemistry : PPB May 2022Brassica juncea var. tumida Tsen et Lee (Tumorous stem mustard) is an unique vegetable in China. Its enlarged tumorous stem was used as main raw material to produce...
Brassica juncea var. tumida Tsen et Lee (Tumorous stem mustard) is an unique vegetable in China. Its enlarged tumorous stem was used as main raw material to produce pickle (Zhacai). In practice, early-bolting happens around 15% of planting area all year and inhibits its production. Here, about 209 PP2C proteins were identified through HMMER software and divided into 13 sub-families in B. juncea. BjuPP2C52 belongs to E sub-family, was up-regulated at reproductive growth stages and interacts with BjuFKF1, a key protein in regulating plant photoperiod flowering, in vitro and in vivo. To explore interactive proteins, BjuPP2C52 was used as bait, 12 potential interactive proteins were screened from yeast library, and they are BjuCOL3, BjuCOL5, BjuAP2, BjuAP2-1, BjuSVP-1, BjuFLC-2, BjuSKP1f, BjuA014572, BjuA008686, BjuO002119, BjuB036787 and BjuA019268. Further study verified that 10 out of the 12 screened proteins interacted with BjuPP2C52 in vivo. qRT-PCR was conducted to understand the expression pattern of those 10 interactive proteins in different tissues and development stages in B. juncea. The results showed that BjuCOL3, BjuCOL5, BjuB036787 and BjuA019268 were significantly up-regulated, while BjuA008686 and BjuO002119 were down-regulated in flowers compared with other four tissues. In developmental stages, BjuCOL5, BjuAP2, BjuAP2-1, BjuA014572, BjuB036787 and BjuA019268 were significantly up-regulated, while BjuSVP-1, BjuA008686 and BjuO002119 were down-regulated at reproductive stages. Based on the results, BjuCOL5, BjuAP2, BjuAP2-1, BjuSVP-1, BjuA014572, BjuB036787 and BjuA019268 may function in regulating flowering time in B. juncea.
Topics: Flowers; Gene Expression Regulation, Plant; Humans; Mustard Plant; Phylogeny; Plant Proteins
PubMed: 35306327
DOI: 10.1016/j.plaphy.2022.03.013 -
Biochemical Society Transactions Apr 2021Asparaginyl endopeptidases (AEPs) are versatile enzymes that in biological systems are involved in producing three different catalytic outcomes for proteins, namely (i)... (Review)
Review
Asparaginyl endopeptidases (AEPs) are versatile enzymes that in biological systems are involved in producing three different catalytic outcomes for proteins, namely (i) routine cleavage by bond hydrolysis, (ii) peptide maturation, including macrocyclisation by a cleavage-coupled intramolecular transpeptidation and (iii) circular permutation involving separate cleavage and transpeptidation reactions resulting in a major reshuffling of protein sequence. AEPs differ in their preference for cleavage or transpeptidation reactions, catalytic efficiency, and preference for asparagine or aspartate target residues. We look at structural analyses of various AEPs that have laid the groundwork for identifying important determinants of AEP function in recent years, with much of the research impetus arising from the potential biotechnological and pharmaceutical applications.
Topics: Catalytic Domain; Cysteine Endopeptidases; Hydrolysis; Molecular Dynamics Simulation; Peptides; Plant Proteins; Protein Binding; Protein Conformation; Seed Storage Proteins; Substrate Specificity
PubMed: 33666219
DOI: 10.1042/BST20200908