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  • 1
    Publication Date: 2009-06-02
    Description: Higher plants produce seed through pollination, using specific interactions between pollen and pistil. Self-incompatibility is an important mechanism used in many species to prevent inbreeding; it is controlled by a multi-allelic S locus. 'Self' (incompatible) pollen is discriminated from 'non-self' (compatible) pollen by interaction of pollen and pistil S locus components, and is subsequently inhibited. In Papaver rhoeas, the pistil S locus product is a small protein that interacts with incompatible pollen, triggering a Ca(2+)-dependent signalling network, resulting in pollen inhibition and programmed cell death. Here we have cloned three alleles of a highly polymorphic pollen-expressed gene, PrpS (Papaver rhoeas pollen S), from Papaver and provide evidence that this encodes the pollen S locus determinant. PrpS is a single-copy gene linked to the pistil S gene (currently called S, but referred to hereafter as PrsS for Papaver rhoeas stigma S determinant). Sequence analysis indicates that PrsS and PrpS are equally ancient and probably co-evolved. PrpS encodes a novel approximately 20-kDa protein. Consistent with predictions that it is a transmembrane protein, PrpS is associated with the plasma membrane. We show that a predicted extracellular loop segment of PrpS interacts with PrsS and, using PrpS antisense oligonucleotides, we demonstrate that PrpS is involved in S-specific inhibition of incompatible pollen. Identification of PrpS represents a major advance in our understanding of the Papaver self-incompatibility system. As a novel cell-cell recognition determinant it contributes to the available information concerning the origins and evolution of cell-cell recognition systems involved in discrimination between self and non-self, which also include histocompatibility systems in primitive chordates and vertebrates.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2699350/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2699350/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wheeler, Michael J -- de Graaf, Barend H J -- Hadjiosif, Natalie -- Perry, Ruth M -- Poulter, Natalie S -- Osman, Kim -- Vatovec, Sabina -- Harper, Andrea -- Franklin, F Christopher H -- Franklin-Tong, Vernonica E -- BB/C501325/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- England -- Nature. 2009 Jun 18;459(7249):992-5. doi: 10.1038/nature08027. Epub 2009 May 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19483678" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Cell Membrane/metabolism ; Gene Expression Regulation, Plant ; Genes, Plant ; Genetic Linkage ; Molecular Sequence Data ; Papaver/*physiology ; Plant Proteins/chemistry/genetics/metabolism ; Pollen/cytology/*physiology ; Pollination/physiology ; Reproduction/physiology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2015-11-07
    Description: Self-incompatibility (SI) is a major genetically controlled system used to prevent inbreeding in higher plants. S determinants regulate allele-specific rejection of "self" pollen by the pistil. SI is an important model system for cell-to-cell recognition and signaling and could be potentially useful for first-generation (F1) hybrid breeding. To date, the transfer of S determinants has used the complementation of orthologs to "restore" SI in close relatives. We expressed the Papaver rhoeas S determinants PrsS and PrpS in Arabidopsis thaliana. This enabled pistils to reject pollen expressing cognate PrpS. Moreover, plants coexpressing cognate PrpS and PrsS exhibit robust SI. This demonstrates that PrsS and PrpS are sufficient for a functional synthetic S locus in vivo. This transfer of novel S determinants into a highly divergent species (〉140 million years apart) with no orthologs suggests their potential utility in crop production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Zongcheng -- Eaves, Deborah J -- Sanchez-Moran, Eugenio -- Franklin, F Christopher H -- Franklin-Tong, Vernonica E -- BB/C501325/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2015 Nov 6;350(6261):684-7. doi: 10.1126/science.aad2983.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26542572" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*physiology ; Crops, Agricultural/genetics/physiology ; Flowers/genetics/physiology ; Gene Expression Regulation, Plant ; Hybridization, Genetic/genetics/*physiology ; Inbreeding ; Papaver/genetics/*physiology ; Plant Proteins/genetics/*physiology ; Pollen/genetics/physiology ; Pollination/genetics/physiology ; Promoter Regions, Genetic ; Self-Incompatibility in Flowering Plants/genetics/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract. Ribonuclease assays have revealed, in contrast to the self-incompatibility (SI) system of Nicotiana alata, there is no detectable ribonuclease activity that correlates with the presence of the functional stigmatic S-gene product in Papaver rhoeas. Thus, we have shown that the inhibition of incompatible pollen tube growth in P. rhoeas is not associated with ribonuclease activity. Furthermore, the finding that pollen from P. rhoeas, unlike that from N. alata, is insensitive to purified bovine pancreatic ribonuclease A at very high concentrations, suggests that the involvement of ribonucleases in the inhibition reaction of the SI response in P. rhoeas is unlikely. In addition, the level of ribonuclease activity in mature stigmas of P. rhoeas is very much lower than that in N. alata and significantly, the level of ribonuclease activity did not rise in conjunction with the developmental expression of SI. Therefore, as a result of these studies, we believe that SI in P. rhoeas does not involve ribonuclease activity.
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  • 4
    ISSN: 1432-0983
    Keywords: Transformation ; Septoria nodorum ; Plant pathogen ; Hygromycin resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The phytopathogenic fungus Septoria nodorum has been transformed using a plasmid (pAN7-1) containing the Escherichia coli hygromycin phosphotransferase gene (hph). Large, stable hygromycin-resistant transformant colonies appeared at frequencies between 2 and 25 per μg DNA when wheat-adapted and barley-adapted wild type strains were used as recipients. These transformants grew at hygromycin concentrations up to ten times that which inhibits the wild types. A second type of colony also developed on transformation plates. These appeared at higher frequencies, grew less vigorously and could not be subcultured in the presence of hygromycin. They are believed to be abortive transformants. Southern hybridization analyses indicated that transformation takes place via the integration of plasmid DNA into the fungal chromosomal DNA. Multiple integrations occur producing tandemly iterated arrays of plasmid molecules. Some transformants arose as heterokaryons. These could be resolved by propagation through a single spore and transformants purified in this way remained mitotically stable. All of 1,025 transformants tested were unchanged in pathogenicity. Reisolates from leaves retained their hygromycin-resistance, indicating that transformants remain stable during growth in plant tissue. Cotransformation of an unselected plasmid (p3SR2) carrying the Aspergillus nidulans amdS gene occurred at a high frequency.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1430-3418
    Keywords: Ca2+ ; Inositol 1,4,5-trisphosphate ; Papaver rhoeas L. ; Pollen ; Second messengers ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A role for cytosolic free Ca2+ (Ca2+i) in the regulation of growth of Papaver rhoeas pollen tubes during the self-incompatibility response has recently been demonstrated [Franklin-Tong et al. Plant J. 4:163–177 (1993); Franklin-Tong et al. Plant J. 8:299–307 (1995); Franklin-Tong et al. submitted to Plant J.]. We have investigated the possibility that Ca2+i is more generally involved in the regulation of pollen tube growth using confocal laser scanning microscopy (CLSM). Data obtained using Ca2+ imaging, in conjunction with photolytic release of caged inositol 1,4,5-trisphosphate [Ins(1,4,5)P3], point to a central role of the phosphoinositide signal transduction pathway in the control of Ca2+ fluxes and control of pollen tube growth. These experiments further revealed that increases in cytosolic levels of Ins(1,4,5)P3 resulted in the formation of distinct Ca2+ waves. Experiments using the pharmacological agents heparin, neomycin and mastoparan further indicated that Ca2+ waves are propagated, at least in part, by Ins(1,4,5)P3-induced Ca2+ release rather than by simple diffusion or by “classic” Ca2+-induced Ca2+ release mechanisms. We also have data which suggest that Ca2+ waves and oscillations may be induced by photolytic release of caged Ca2+. Ratio-imaging has enabled us to identify an apical oscillating Ca2+ gradient in growing pollen tubes, which may regulate normal pollen tube growth. We also present evidence for the involvement of Ca2+ waves in mediating the self-incompatibility response. Our data suggest that changes in Ca2+i and alterations in growth rate/patterns are likely to be closely correlated and may be causally linked to events such as Ca2+-induced, or Ins(1,4,5)P3-induced wave formation and apical Ca2+ oscillations.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Sexual plant reproduction 12 (2000), S. 310-313 
    ISSN: 1432-2145
    Keywords: Key words Meiosis ; Arabidopsis ; Pelota
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  We have identified a plant homologue of the Drosophila meiotic gene Pelota in Arabidopsis thaliana (AtPelota1). This gene maps to chromosome 4 of Ara- bidopsis and is one of two Pelota homologues present in this plant. When the expression pattern of AtPelota1 was examined it was found to be expressed at similar levels in all plant tissues tested (whole plant, bud, stem, leaf and root). This expression pattern corresponds to that seen for some other Arabidopsis meiotic genes and their homologues. A search of the databases reveal that the AtPelota gene family is widespread with homologues present in higher and lower eukaryotes and archaebacteria, but not eubacteria.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 110 (1976), S. 287-293 
    ISSN: 1432-072X
    Keywords: d-Alanine ; l-Alanine ; β-Alanine ; Dehydrogenase ; Oxidase ; Pseudomonas aeruginosa ; Catabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pseudomonas aeruginosa PA01 was found to utilise both thed- andl-isomers of α-alanine and also β-alanine as sole sources of carbon and energy for growth. Enzymological studies of wild-type cultures and comparison with mutants deficient in growth upon one or more isomers of alanine led to the following conclusions: (i) utilisation ofd-alanine involved its direct oxidation by an inducible, membrane-bound, cytochrome-linked dehydrogenase; (ii) utilisation ofl-alanine required its conversion to the directly oxidisabled-form by a soluble racemase; (iii) utilisation of β-alanine, likel-alanine, involves both the racemase andd-alanine dehydrogenase enzymes, but in addition must involve other enzymes the identity, of which is still speculative; (iv)P. aeruginosa, likeEscherichia coli, appears to take upd-alanine andl-alanine by means of two specific permeases.
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  • 8
    ISSN: 1573-5028
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1573-5028
    Keywords: self-incompatibility ; Papaver rhoeas ; S gene ; homologous alleles ; recombinant S protein ; pollen inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The S 3 allele of the S gene has been cloned from Papaver rhoeas cv. Shirley. The sequence predicts a hydrophilic protein of 14.0 kDa, showing 55.8% identity with the previously cloned S 1 allele, preceded by an 18 amino acid signal sequence. Expression of the S 3 coding region in Escherichia coli produced a form of the protein, denoted S3e, which specifically inhibited S3 pollen in an in vitro bioassay. The recombinant protein was ca. 0.8 kDa larger than the native stigmatic form, indicating post-translational modifications in planta, as was previously suggested for the S1 protein. In contrast to other S proteins identified to date, S3 protein does not appear to be glycosylated. Of particular significance is the finding that despite exhibiting a high degree of sequence polymorphism, secondary structure predictions indicate that the S1 and S3 proteins may adopt a virtually identical conformation. Sequence analysis also indicates that the P. rhoeas S alleles share some limited homology with the SLG and SRK genes from Brassica oleracea. Previously, cross-classification of different populations of P. rhoeas had revealed a number of functionally identical alleles. Probing of western blots of stigma proteins from plants derived from a wild Spanish population which contained an allele functionally identical to the Shirley S 3 allele with antiserum raised to S3e, revealed a protein (S 3 s) which was indistinguishable in pI and M r from that in the Shirley population. A cDNA encoding S 3 s was isolated, nucleotide sequencing revealing a coding region with 99.4% homology with the Shirley-derived clone at the DNA level, and 100% homology at the amino acid level.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 149 (1976), S. 229-237 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary E. coli K12 was found to utilise both D-and L-stereoisomers of alanine as sole sources of carbon, nitrogen and energy for growth. This capability was absolutely dependent upon the possession of an active membrane-bound D-alanine dehydrogenase, and was lost by mutants in which the enzyme was defective. The Michaelis constant for the enzyme with D-alanine as substrate was 30 mM, and the pH optimum about 8.9. D-alanine was the most active substrate, L-alanine was inactive and several other D-amino acids were 10–50% as active as D-alanine. Oxidation of D-alanine was linked to oxygen via a cytochrome-containing respiratory chain. Synthesis of the dehydrogenase was induced 16 to 23-fold by incubation with D-or L-alanine, but only D-alanine was intrinsically active as an inducer. L-alanine was active either as a substrate or inducer only in the presence of an uninhibited alanine racemase which converted it to the D-isomer. The map-location of their structural genes between ara and leu, together with other similarities, indicate that D-alanine dehydrogenase and the “alaninase” of Wijsman (1972a) are the same enzyme. Both D-and L-alanine were intrinsically active as inducers of alanine racemase synthesis. The synthesis of both D-alanine dehydrogenase and alanine racemase was found to be regulated by catabolite repression.
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