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1.
Science ; 361(6403)2018 08 17.
Article in English | MEDLINE | ID: mdl-30115782

ABSTRACT

The coordinated expression of highly related homoeologous genes in polyploid species underlies the phenotypes of many of the world's major crops. Here we combine extensive gene expression datasets to produce a comprehensive, genome-wide analysis of homoeolog expression patterns in hexaploid bread wheat. Bias in homoeolog expression varies between tissues, with ~30% of wheat homoeologs showing nonbalanced expression. We found expression asymmetries along wheat chromosomes, with homoeologs showing the largest inter-tissue, inter-cultivar, and coding sequence variation, most often located in high-recombination distal ends of chromosomes. These transcriptionally dynamic genes potentially represent the first steps toward neo- or subfunctionalization of wheat homoeologs. Coexpression networks reveal extensive coordination of homoeologs throughout development and, alongside a detailed expression atlas, provide a framework to target candidate genes underpinning agronomic traits in wheat.


Subject(s)
Gene Expression Regulation, Plant , Polyploidy , Transcription, Genetic , Triticum/genetics , Bread , Gene Expression Profiling , Gene Expression Regulation, Developmental , Genome, Plant , RNA, Plant/genetics , Sequence Analysis, RNA , Triticum/growth & development
2.
Mol Plant Microbe Interact ; 27(10): 1095-106, 2014 Oct.
Article in English | MEDLINE | ID: mdl-24964059

ABSTRACT

This study investigated the impact of brassinosteroid (BR)-insensitive 1 (BRI1) mutation, the main receptor of BR in both Brachypodium distachyon and barley, on disease resistance against a range of fungal pathogens of cereals exhibiting different trophic lifestyles. Results presented here show that i) disruption of BRI1 has pleiotropic effects on disease resistance in addition to affecting plant development. BR signaling functions antagonistically with mechanisms of disease resistance that are effective against a broad range of cereal pathogens. ii) Disruption of BRI1 results in increased disease resistance against necrotrophic and hemibiotrophic pathogens that exhibit only a marginal asymptomatic phase but has no effect on biotrophic pathogens or those with a prolonged asymptomatic phase, and iii) disruption of BRI1 has a similar effect on disease resistance in B. distachyon and barley, indicating that defense mechanisms are conserved between these species. This work presents the first evidence for conservation of disease resistance mechanisms between the model species B. distachyon and the cereal crop barley and validates B. distachyon for undertaking model-to-crop translation studies of disease resistance.


Subject(s)
Ascomycota/physiology , Brachypodium/genetics , Fusarium/physiology , Hordeum/immunology , Plant Diseases/immunology , Plant Proteins/genetics , Brachypodium/microbiology , Chromosomes, Plant/genetics , Disease Resistance , Flowers/immunology , Flowers/microbiology , Hordeum/microbiology , Mutation , Plant Diseases/microbiology , Plant Leaves/immunology , Plant Leaves/microbiology , Plant Proteins/metabolism , Plant Roots/immunology , Plant Roots/microbiology , Seedlings/immunology , Seedlings/microbiology
3.
Hum Mutat ; 29(3): 451, 2008 Mar.
Article in English | MEDLINE | ID: mdl-18273899

ABSTRACT

A nonsense mutation (c.729C>A, Y243X) in exon 7 of the PDHA1 gene in a patient with pyruvate dehydrogenase deficiency results in aberrant splicing of the primary transcript with production of stable mRNAs which lack either both exons 6 and 7 or exon 7 alone. Transfection and expression of genomic constructs covering exons 5 to 8 of the mutant PDHA1 gene reproduced this aberrant splicing in vitro. The same pattern of abnormal splicing was found when a silent mutation was introduced at the same position. Both the nonsense and silent mutations alter a strong consensus site for the binding of SRp40, suggesting that they may interfere with an exonic splicing enhancer in exon 7 of the gene. However, this appears to affect splicing of not only exon 7, but also the adjacent upstream exon. The splice acceptor site of intron 5 has weak homology to the consensus sequence and this may contribute to the combined splicing defect.


Subject(s)
Codon, Nonsense , Enhancer Elements, Genetic , Pyruvate Dehydrogenase (Lipoamide)/genetics , RNA Splicing/genetics , Animals , Base Sequence , COS Cells , Cells, Cultured , Chlorocebus aethiops , DNA/genetics , Exons , Genetic Vectors , Humans , Mutagenesis, Site-Directed , Pyruvate Dehydrogenase Complex Deficiency Disease/enzymology , Pyruvate Dehydrogenase Complex Deficiency Disease/genetics , RNA, Messenger/genetics , RNA, Messenger/metabolism , Transfection
4.
Fungal Genet Biol ; 36(2): 98-106, 2002 Jul.
Article in English | MEDLINE | ID: mdl-12081463

ABSTRACT

A mutation of glycine to alanine at position 143 in the mitochondrial cytochrome b amino acid sequence of Blumeria graminis f. sp. tritici cosegregated with the QoI-resistant phenotype in a ratio of 1:1 in a cross between a sensitive and a resistant isolate. This mutation was used as a mitochondrial marker to determine whether mitochondrial inheritance in B. graminis was anisogamous, as in heterothallic Neurospora sp., or isogamous and hermaphroditic, as in Aspergillus nidulans. Segregation of mitochondrial genotypes in B. graminis f. sp. tritici was consistent with inheritance of mitochondria being hermaphroditic and isogamous, in that all ascospores from an individual cleistothecium had the same mitochondrial genotype and that either parent could act as the maternal parent of a cleistothecium. Within each cleistothecium, nuclear segregation occurred independently of mitochondrial inheritance, as shown by segregation of resistance to the fungicide triadimenol and by segregation of avirulences to the wheat cultivars Galahad (Pm2), Armada (Pm4b), and Holger (Pm6).


Subject(s)
Cytochrome b Group/genetics , Drug Resistance, Fungal/genetics , Fungi/genetics , Amino Acid Sequence , Antifungal Agents/metabolism , Antifungal Agents/pharmacology , Crosses, Genetic , Fungi/pathogenicity , Fungi/ultrastructure , Mitochondria/drug effects , Mitochondria/genetics , Molecular Sequence Data , Point Mutation , Sequence Alignment , Triazoles , Triticum , Virulence
5.
Structure ; 3(11): 1225-33, 1995 Nov 15.
Article in English | MEDLINE | ID: mdl-8591033

ABSTRACT

BACKGROUND: Cytochrome c peroxidase from Pseudomonas aeruginosa (PsCCP) represents a new class of peroxidases which work without the need to create a semi-stable free radical for catalysis. The enzyme is located in the bacterial periplasm where its likely function is to provide protection against toxic peroxides. The soluble 323-residue single polypeptide chain contains two covalent c-type haems with very different properties: one of them is a low-potential (-330 mV) centre where hydrogen peroxide is reduced (the peroxidatic site); the other is a high-potential (+320 mV) centre which feeds electrons to the peroxidatic site from soluble electron-shuttle proteins such as cytochrome c and azurin. RESULTS: The crystal structure of the oxidized form of PsCCP has been determined to 2.4 A resolution by multiple isomorphous replacement, and refined to an R-factor of 19.2%. PsCCP is organized into two domains, both of them containing a covalent c-haem in a structure reminiscent of class 1 cytochromes c. The domains are related by a quasi-twofold axis. The domain interface holds a newly discovered calcium-binding site with an unusual set of ligands. CONCLUSIONS: The likely function of the calcium site is to maintain the structural integrity of the enzyme and/or to modulate electron transfer between the two haem domains. The low-potential haem has two histidine axial ligands (His55 and His71) and the high-potential haem is ligated by His201 and Met275. There are no polar residues at the peroxidatic site in the inactive oxidized enzyme. The structure suggests that, in the half-reduced functional form of the enzyme, the low-potential haem has to shed His71 in order to make the enzyme catalytically competent. This process is likely to trigger a reorganization of the active site, and may introduce a new residues into the haem pocket.


Subject(s)
Bacterial Proteins/chemistry , Cytochrome-c Peroxidase/chemistry , Models, Molecular , Protein Conformation , Pseudomonas aeruginosa/enzymology , Amino Acid Sequence , Binding Sites , Calcium/metabolism , Catalysis , Crystallography, X-Ray , Electron Transport , Free Radicals , Heme/chemistry , Iron/chemistry , Molecular Sequence Data , Oxidation-Reduction , Peroxidases/classification , Structure-Activity Relationship
6.
FEBS Lett ; 365(2-3): 152-4, 1995 May 29.
Article in English | MEDLINE | ID: mdl-7781769

ABSTRACT

The nucleotide sequence of the gene encoding cytochrome c551 peroxidase from Pseudomonas aeruginosa is reported. The translated amino acid sequence differs from the sequence reported earlier by peptide mapping most significantly by the presence of a section containing an additional 20 residues. A number of minor differences are also evident. The new sequence translates to a protein containing 346 amino acids, the first 23 being typical of a hydrophobic leader peptide with a characteristic protease cleavage site.


Subject(s)
Bacterial Proteins , Cytochrome-c Peroxidase/biosynthesis , Cytochrome-c Peroxidase/genetics , Pseudomonas aeruginosa/enzymology , Pseudomonas aeruginosa/genetics , Amino Acid Sequence , Animals , Base Sequence , Blotting, Southern , Cloning, Molecular , Cytochrome c Group/metabolism , Escherichia coli/genetics , Manduca/genetics , Molecular Sequence Data , Oligodeoxyribonucleotides , Recombinant Proteins/biosynthesis , Restriction Mapping , Sequence Homology, Amino Acid
7.
Toxicol In Vitro ; 3(2): 85-90, 1989.
Article in English | MEDLINE | ID: mdl-20702304

ABSTRACT

The effect of a range of saponins, commonly present in foods or dietary supplements, on the potential difference (PD) across the mucosa of the rat small intestine in vitro has been examined. Saponins from Gypsophila, guar, alfalfa, Quillaja, clover and liquorice together with glycoalkaloids from the potato and tomato were examined. The typical response was an immediate reduction in PD, although there was considerable variation in the response to particular compounds. Amongst the factors affecting the nature and magnitude of the de-polarizing effect were pH, solubility and the chemical form of the saponin. In agreement with the findings of others, glycyrrhizic acid, isolated from liquorice root, was found to exhibit a protective effect against the activity of a more potent saponin. The observations are discussed in the light of the known physiological activities of plant saponins and the regular, or excessive, consumption of certain foods or dietary supplements.

9.
Pharm Acta Helv ; 43(1): 42-9, 1968 Jan.
Article in English | MEDLINE | ID: mdl-5719456
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