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Biochimica Et Biophysica Acta Jun 2009The chlorophyll a/b light-harvesting complex of photosystem II (LHC-II) collects most of the solar energy in the biosphere. LHC-II is the prototype of a highly conserved... (Review)
Review
The chlorophyll a/b light-harvesting complex of photosystem II (LHC-II) collects most of the solar energy in the biosphere. LHC-II is the prototype of a highly conserved family of membrane proteins that fuels plant photosynthesis in the conversion of excitation energy into biologically useful chemical energy. In addition, LHC-II plays an important role in the organisation of the thylakoid membrane, the structure of the photosynthetic apparatus, the regulation of energy flow between the two photosystems, and in the controlled dissipation of excess excitation energy under light stress. Our current understanding of the sophisticated mechanisms behind each of these processes has profited greatly from the progress made over the past two decades in determining the structure of the complex. This review presents the developments and breakthroughs that ultimately lead to the high-resolution structure of LHC-II. Based on an alignment of the remarkably well engineered and highly conserved LHC polypeptide, we propose several key features of the LHC-II structure that are likely to be present in all members of the LHC family. Finally, some recently proposed mechanisms of energy-dependent non-photochemical quenching (NPQ) are examined from a structural perspective.
Topics: Amino Acid Sequence; Arabidopsis Proteins; Binding Sites; Crystallization; Crystallography, X-Ray; Freeze Fracturing; Light-Harvesting Protein Complexes; Microscopy, Electron, Transmission; Models, Molecular; Molecular Sequence Data; Photochemical Processes; Photosystem II Protein Complex; Plant Proteins; Protein Structure, Quaternary; Sequence Homology, Amino Acid
PubMed: 19327340
DOI: 10.1016/j.bbabio.2009.03.012 -
BMC Genomics Jun 2020Multiple C2 domains and transmembrane region proteins (MCTPs) may act as transport mediators of other regulators. Although increased number of MCTPs in higher plants...
BACKGROUND
Multiple C2 domains and transmembrane region proteins (MCTPs) may act as transport mediators of other regulators. Although increased number of MCTPs in higher plants implies their diverse and specific functions in plant growth and development, only a few plant MCTPs have been studied and no study on the MCTPs in cotton has been reported.
RESULTS
In this study, we identified 31 MCTPs in G. hirsutum, which were classified into five subfamilies according to the phylogenetic analysis. GhMCTPs from subfamily V exhibited isoelectric points (pIs) less than 7, whereas GhMCTPs from subfamily I, II, III and IV exhibited pIs more than 7.5, implying their distinct biological functions. In addition, GhMCTPs within subfamily III, IV and V exhibited more diverse physicochemical properties, domain architectures and expression patterns than GhMCTPs within subfamily I and II, suggesting that GhMCTPs within subfamily III, IV and V diverged to perform more diverse and specific functions. Analyses of conserved motifs and pIs indicated that the N-terminus was more divergent than the C-terminus and GhMCTPs' functional divergence might be mainly contributed by the N-terminus. Furthermore, yeast two-hybrid assay indicated that the N-terminus was responsible to interact with target proteins. Phylogenetic analysis classified multiple N-terminal C2 domains into four subclades, suggesting that these C2 domains performed different molecular functions in mediating the transport of target proteins.
CONCLUSIONS
Our systematic characterization of MCTPs in G. hirsutum will provide helpful information to further research GhMCTPs' molecular roles in mediating other regulators' transport to coordinate growth and development of various cotton tissues.
Topics: Binding Sites; Chromosome Mapping; Gossypium; Membrane Proteins; Multigene Family; Phylogeny; Plant Proteins; Protein Domains; Whole Genome Sequencing
PubMed: 32600247
DOI: 10.1186/s12864-020-06842-1 -
International Journal of Molecular... Nov 2012The heat shock protein 90 (Hsp90) family mediates stress signal transduction, and plays important roles in the control of normal growth of human cells and in promoting... (Review)
Review
The heat shock protein 90 (Hsp90) family mediates stress signal transduction, and plays important roles in the control of normal growth of human cells and in promoting development of tumor cells. Hsp90s have become a currently important subject in cellular immunity, signal transduction, and anti-cancer research. Studies on the physiological functions of Hsp90s began much later in plants than in animals and fungi. Significant progress has been made in understanding complex mechanisms of HSP90s in plants, including ATPase-coupled conformational changes and interactions with cochaperone proteins. A wide range of signaling proteins interact with HSP90s. Recent studies revealed that plant Hsp90s are important in plant development, environmental stress response, and disease and pest resistance. In this study, the plant HSP90 family was classified into three clusters on the basis of phylogenetic relationships, gene structure, and biological functions. We discuss the molecular functions of Hsp90s, and systematically review recent progress of Hsp90 research in plants.
Topics: HSP90 Heat-Shock Proteins; Plant Proteins; Plants; Stress, Physiological
PubMed: 23443089
DOI: 10.3390/ijms131215706 -
Microbes and Infection Apr 2007Both plant and animal genomes encode proteins with nucleotide binding domains fused to leucine-rich repeat domains that are involved in responses to pathogens. While... (Review)
Review
Both plant and animal genomes encode proteins with nucleotide binding domains fused to leucine-rich repeat domains that are involved in responses to pathogens. While these domain structures are probably an example of convergent evolution, there are a number of similarities in the core mechanisms by which these proteins are regulated.
Topics: Adaptor Proteins, Signal Transducing; Animals; Immunity, Innate; Plant Proteins; Repressor Proteins; Signal Transduction
PubMed: 17379561
DOI: 10.1016/j.micinf.2007.01.019 -
BMC Bioinformatics Jul 2005Recognition of microbial pathogens by plants triggers the hypersensitive reaction, a common form of programmed cell death in plants. These dying cells generate signals...
BACKGROUND
Recognition of microbial pathogens by plants triggers the hypersensitive reaction, a common form of programmed cell death in plants. These dying cells generate signals that activate the plant immune system and alarm the neighboring cells as well as the whole plant to activate defense responses to limit the spread of the pathogen. The molecular mechanisms behind the hypersensitive reaction are largely unknown except for the recognition process of pathogens. We delineate the NRP-gene in soybean, which is specifically induced during this programmed cell death and contains a novel protein domain, which is commonly found in different plant proteins.
RESULTS
The sequence analysis of the protein, encoded by the NRP-gene from soybean, led to the identification of a novel domain, which we named DCD, because it is found in plant proteins involved in development and cell death. The domain is shared by several proteins in the Arabidopsis and the rice genomes, which otherwise show a different protein architecture. Biological studies indicate a role of these proteins in phytohormone response, embryo development and programmed cell by pathogens or ozone.
CONCLUSION
It is tempting to speculate, that the DCD domain mediates signaling in plant development and programmed cell death and could thus be used to identify interacting proteins to gain further molecular insights into these processes.
Topics: Amino Acid Motifs; Cell Death; Phylogeny; Plant Proteins; Protein Structure, Tertiary; Sequence Analysis, Protein; Glycine max
PubMed: 16008837
DOI: 10.1186/1471-2105-6-169 -
Scientific Reports Nov 2017Abscisic acid (ABA), stress and ripening (ASR) proteins are plant-specific proteins involved in plant response to multiple abiotic stresses. We previously isolated the...
Abscisic acid (ABA), stress and ripening (ASR) proteins are plant-specific proteins involved in plant response to multiple abiotic stresses. We previously isolated the ASR genes and cDNAs from durum wheat (TtASR1) and barley (HvASR1). Here, we show that HvASR1 and TtASR1 are consistently predicted to be disordered and further confirm this experimentally. Addition of glycerol, which mimics dehydration, triggers a gain of structure in both proteins. Limited proteolysis showed that they are highly sensitive to protease degradation. Addition of 2,2,2-trifluoroethanol (TFE) however, results in a decreased susceptibility to proteolysis that is paralleled by a gain of structure. Mass spectrometry analyses (MS) led to the identification of a protein fragment resistant to proteolysis. Addition of zinc also induces a gain of structure and Hydrogen/Deuterium eXchange-Mass Spectrometry (HDX-MS) allowed identification of the region involved in the disorder-to-order transition. This study is the first reported experimental characterization of HvASR1 and TtASR1 proteins, and paves the way for future studies aimed at unveiling the functional impact of the structural transitions that these proteins undergo in the presence of zinc and at achieving atomic-resolution conformational ensemble description of these two plant intrinsically disordered proteins (IDPs).
Topics: Abscisic Acid; Hordeum; Intrinsically Disordered Proteins; Plant Proteins; Protein Folding; Proteolysis; Stress, Physiological; Triticum
PubMed: 29138428
DOI: 10.1038/s41598-017-15299-4 -
Current Opinion in Plant Biology Aug 2010In plants, many of the innate immune receptors or disease resistance (R) proteins contain a NB-LRR (Nucleotide-binding site, Leucine-rich repeat) structure. The recent... (Review)
Review
In plants, many of the innate immune receptors or disease resistance (R) proteins contain a NB-LRR (Nucleotide-binding site, Leucine-rich repeat) structure. The recent findings regarding NB-LRR signaling are summarized in this article. An emerging theme is that two NB-LRRs can function together to mediate disease resistance against pathogen isolates. Also, recent results delineate the NB-LRR protein fragments that are sufficient to initiate defense signaling. Importantly, distinct fragments of different NB-LRRs are sufficient for function. Finally, we describe the new roles of accessory proteins and downstream host genes in NB-LRR signaling.
Topics: Animals; Binding Sites; Humans; Nucleotides; Plant Diseases; Plant Proteins; Repetitive Sequences, Amino Acid; Signal Transduction
PubMed: 20483655
DOI: 10.1016/j.pbi.2010.04.007 -
The Plant Journal : For Cell and... Apr 1999The cycloidea (cyc) and teosinte branched 1 (tb1) genes code for structurally related proteins implicated in the evolution of key morphological traits. However, the...
The cycloidea (cyc) and teosinte branched 1 (tb1) genes code for structurally related proteins implicated in the evolution of key morphological traits. However, the biochemical function of CYC and TB1 proteins remains to be demonstrated. To address this problem, we have analysed the predicted secondary structure of regions conserved between CYC and TB1, and looked for related proteins of known function. One of the conserved regions is predicted to form a non-canonical basic-Helix-Loop-Helix (bHLP) structure. This domain is also found in two rice DNA-binding proteins, PCF1 and PCF2, where it has been shown to be involved in DNA-binding and dimerization. This indicates that the conserved domain most probably defines a new family of transcription factors, which we have termed the TCP family after its first characterised members (TB1, CYC and PCFs). Other plant proteins of unknown function also belong to this family. We have studied two of these in Arabidopsis and have shown that they are expressed in rapidly growing floral primordia. This, together with the proposed involvement of cyc and tb1 in influencing meristem growth, suggests that many members of the TCP family may affect cell division. Some of these genes may have been recruited during plant evolution to generate new morphological traits.
Topics: Amino Acid Sequence; Base Sequence; DNA, Complementary; Helix-Loop-Helix Motifs; Molecular Sequence Data; Plant Development; Plant Proteins; Protein Structure, Secondary
PubMed: 10363373
DOI: 10.1046/j.1365-313x.1999.00444.x -
Molecular Plant Jul 2012
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Plant Physiology Aug 2022Plants have evolved different routes for the synthesis and assembly of the building blocks of proanthocyanidins.
Plants have evolved different routes for the synthesis and assembly of the building blocks of proanthocyanidins.
Topics: Gene Expression Regulation, Plant; Plant Proteins; Proanthocyanidins
PubMed: 35695780
DOI: 10.1093/plphys/kiac274