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  • Ribosomal protein  (3)
  • 12.38.Lg  (2)
  • Arabidopsis  (2)
  • Cardiovascular tissues  (2)
  • Springer  (9)
  • 1995-1999  (9)
Collection
Keywords
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  • Springer  (9)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    QCD sum rules with finite masses (1995)
    Springer
    The European physical journal 351 (1995), S. 345-351 
    Details
    ISSN: 1434-601X
    Keywords: 12.38.-t ; 12.38.Lg ; 14.65.-q
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The concept of QCD sum rules is extended to bound states composed of particles with finite mass such as scalar quarks or strange quarks. It turns out that mass corrections become important in this context. The number of relevant corrections is analyzed in a systematic discussion of the IR- and UV-divergencies, leading in general to a finite number of corrections. The results are demonstrated for a system of two massless quarks and two heavy scalar quarks.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01290918
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  • 2
    Electronic Resource
    Electronic Resource
    Diffractive meson production and the quark-pomeron coupling (1995)
    Springer
    The European physical journal 352 (1995), S. 203-210 
    Details
    ISSN: 1434-601X
    Keywords: 12.40.−y ; 12.40.Gg ; 12.38.Lg
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Diffractive meson production at HERA offers interesting possibilities to investigate diffractive processes and thus to learn something about the properties of the pomeron. The most succesful phenomenological description of the pomeron so far assumes it to couple like a C=+1 isoscalar photon to single quarks. This coupling leads, however, to problems for exclusive diffractive reactions. We propose a new phenomenological pomeron vertex, which leads to very good fits to the known data, but avoids the problems of the old vertex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01298909
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  • 3
    Electronic Resource
    Electronic Resource
    The light-induced reduction of the gravitropic growth-orientation of seedlings of Arabidopsis thaliana (L.) Heynh. is a photomorphogenic response mediated synergistically by the far-red-absorbing forms of phytochromes A and B (1996)
    Springer
    Planta 199 (1996), S. 511-514 
    Details
    ISSN: 1432-2048
    Keywords: Arabidopsis ; Gravitropism ; phyB-1 ; Phytochrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Hypocotyls of dark-grown seedlings of Ara bidosis thaliana exhibit a strong negative gravitropism, which is reduced by red and also by long-wavelength, far-red light treatments. Light treatments using phytochrome A (phyA)- and phytochrome B (phyB)-deficient mutants showed that this response is controlled by phyB in a red/far-red reversible way, and by phyA in a non-reversible, very-low-fluence response. Crosses of the previously analyzed phyB-1 allele (in the ecotype Landsberg erecta background) to the ecotype Nossen wild-type (WT) background resulted in a WT-like negative gravitropism in darkness, indicating that the previously described gravitropic randomization observed with phyB-1 in the dark is likely due to a second mutation independent of that in the PHYB gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00195180
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  • 4
    Electronic Resource
    Electronic Resource
    Promoter elements of the mustard CHS1 gene are sufficient for light regulation in transgenic plants (1995)
    Springer
    Plant molecular biology 28 (1995), S. 219-229 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis ; chalcone synthase (expression) ; cis-acting elements (light, organ specifity) ; mustard (Sinapis alba L.) ; tobacco (Nicotiana tabacum) ; transgenic plants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The expression of chalcone synthase (CHS) genes, which encode the first enzyme of the flavonoid pathway, is under developmental control as well as affected by external stimuli such as light. Varying fragments of the 1 kb upstream region of the CHS1 gene from white mustard (Sinapis alba L.) were fused to the GUS-coding region, and the light-regulated expression of these constructs was analysed in transgenic Arabidopsis and tobacco plants. Studies performed with Arabidopsis seedlings indicate the presence of two elements within the CHS1 promoter mediating light responses via different photoreceptors. One element, located about 150 bp upstream of the transcription start site, is homologous to Unit 1 of the parsley CHS gene, the second, far more upstream element carries sequences similar to Unit 2 of the same gene. Detailed studies on Unit 1-driven expression indicate that this element transfers the expression characteristics of the original gene to both Arabidopsis and tobacco. Although the expression characteristics of Unit 1 are indistinguishable from those of the full-length promoter within the same species, we observed differences in mustard CHS promoter regulation between Arabidopsis and tobacco plants transgenic for the identical construct. The difference in photoreceptor usage by the same promoter element in different transgenic species (Unit 1 from mustard in Arabidopsis vs. tobacco) was also observed for different but homologous promoter elements in the same transgenic species (Unit 1 from mustard and parsley in tobacco). We therefore conclude that the same promoter and even the same promoter element (Unit 1) can mediate different spatial patterns of expression and modes of light regulation in different transgenic species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00020242
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  • 5
    Electronic Resource
    Electronic Resource
    The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates (1995)
    Springer
    Cell & tissue research 279 (1995), S. 539-549 
    Details
    ISSN: 1432-0878
    Keywords: Key words: In situ hybridization ; Immunohistochemistry ; Pro-hormone convertases ; Cardiovascular tissues ; Pro-atrial natriuretic factor ; Pro-endothelin ; Processing ; Rat (Sprague Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The present study examined the distribution of the pro-hormone convertases PC1, PC2, furin, PACE4 and PC5 in the rat heart. Northern blot analysis of RNA extracted from cardiac tissues showed high levels of furin and PACE4 mRNA in the atria and ventricles, while PC5 mRNA was found to be expressed at high levels in the dorsal aorta. Although undetectable by Northern blot analysis, both PC1 and PC2 mRNA were detected by in situ hybridization and immunohistochemistry in discrete regions of the intracardiac para-aortic ganglia. In situ hybridization studies also showed that furin mRNA was observed in all cardiac tissues and cells, consistent with the previously reported ubiquitous expression of this gene. PACE4 mRNA was highly abundant in both the atria and ventricular cardiomyocytes, with low to undetectable levels observed in blood vessels. Finally, PC5 transcripts were expressed in the endothelial cells lining coronary vessels and the valve leaflets of the heart. The present localization studies in the heart and cardiac blood vessels suggests potential roles for each convertase in the processing of various neuropeptides, hormones and growth factors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050313
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  • 6
    Electronic Resource
    Electronic Resource
    The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates (1995)
    Springer
    Cell & tissue research 279 (1995), S. 539-549 
    Details
    ISSN: 1432-0878
    Keywords: In situ hybridization ; Immunohistochemistry ; Pro-hormone convertases ; Cardiovascular tissues ; Pro-atrial natriuretic factor ; Pro-endothelin ; Processing ; Rat (Sprague Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The present study examined the distribution of the pro-hormone convertases PC1, PC2, furin, PACE4 and PC5 in the rat heart. Northern blot analysis of RNA extracted from cardiac tissues showed high levels of furin and PACE4 mRNA in the atria and ventricles, while PC5 mRNA was found to be expressed at high levels in the dorsal aorta. Although undetectable by Northern blot analysis, both PC1 and PC2 mRNA were detected by in situ hybridization and immunohistochemistry in discrete regions of the intracardiac para-aortic ganglia. In situ hybridization studies also showed that furin mRNA was observed in all cardiac tissues and cells, consistent with the previously reported ubiquitous expression of this gene. PACE4 mRNA was highly abundant in both the atria and ventricular cardiomyocytes, with low to undetectable levels observed in blood vessels. Finally, PC5 transcripts were expressed in the endothelial cells lining coronary vessels and the valve leaflets of the heart. The present localization studies in the heart and cardiac blood vessels suggests potential roles for each convertase in the processing of various neuropeptides, hormones and growth factors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318166
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  • 7
    Electronic Resource
    Electronic Resource
    A newly identified Minute locus, M(2)32D, encodes the ribosomal protein L9 in Drosophila melanogaster (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 381-387 
    Details
    ISSN: 1617-4623
    Keywords: Key words Drosophila melanogaster ; Minute ; Ribosomal protein ; Mutant rescue
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  A gene encoding a ubiquitously expressed mRNA in Drosophila melanogaster was isolated and identified as the gene for ribosomal protein L9 (rpL9) by its extensive sequence homology to the corresponding gene from rat. The rpL9 gene is localized in polytene region 32D where two independent P element insertions flanking the locus are available. Remobilization of either P element generated lines with a typical Minute phenotype, e.g. thin and short bristles, prolonged development, and female semisterility in heterozygotes as well as homozygous lethality. All these characteristics can be rescued when a 3.9 kb restriction fragment containing the rpL9 gene is reintroduced by P element-mediated germline transformation. This result confirms that M(2)32D codes for ribosomal protein L9.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172530
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  • 8
    Electronic Resource
    Electronic Resource
    A newly identifiedMinute locus,M(2)32D, encodes the ribosomal protein L9 inDrosophila melanogaster (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 381-387 
    Details
    ISSN: 1617-4623
    Keywords: Drosophila melanogaster ; Minute ; Ribosomal protein ; Mutant rescue
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A gene encoding a ubiquitously expressed mRNA inDrosophila melanogaster was isolated and identified as the gene for ribosomal protein L9 (rpL9) by its extensive sequence homology to the corresponding gene from rat. TherpL9 gene is localized in polytene region 32D where two independent P element insertions flanking the locus are available. Remobilization of either P element generated lines with a typicalMinute phenotype, e.g. thin and short bristles, prolonged development, and female semisterility in heterozygotes as well as homozygous lethality. All these characteristics can be rescued when a 3.9 kb restriction fragment containing therpL9 gene is reintroduced by P element-mediated germline transformation. This result confirms thatM(2)32D codes for ribosomal protein L9.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172530
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  • 9
    Electronic Resource
    Electronic Resource
    Relocation of urf a from the mitochondrion to the nucleus cures the mitochondrial mutator phenotype in the fission yeast Schizosaccharomyces pombe (1998)
    Springer
    Molecular genetics and genomics 258 (1998), S. 389-396 
    Details
    ISSN: 1617-4623
    Keywords: Key words Fission yeast ; Ectopic expression ; var1 gene ; Mutator ; Ribosomal protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In previous papers we have reported the characterisation of mitochondrial mutator mutants of Schizosaccharomyces pombe. In contrast to nuclear mutator mutants known from other eucaryotes, this mutator phenotype correlates with mutations in an unassigned open reading frame (urf a) in the mitochondrial genome. Since an efficient biolistic transformation system for fission yeast mitochondria is not yet available, we relocated the mitochondrial urf a gene to the nucleus. As host strain for the ectopic expression, we used the nonsense mutant ana r -6, which carries a premature stop codon in the urf a gene. The phenotype of this mutant is characterised by continuous segregation of progeny giving rise to fully respiration competent colonies, colonies that show moderate growth on glycerol and a fraction of colonies that are unable to grow on glycerol. The phenotype of this mutant provides an excellent tool with which to study the effects on the mutator phenotype of ectopic expression of the urf a gene. Since a UGA codon encoding tryptophan is present in the original mitochondrial gene, we constructed two types of expression cassettes containing either the mitochondrial version of the urf a gene (mt-urf a) or a standard genetic code version (nc-urf a; UGA replaced by UGG) fused to the N-terminal import leader sequence of the cox4 gene of Saccharomyces cerevisiae. We show that the expression of the mt-urf a gene in its new location is able to cure, at least in part, the phenotype of mutant ana r -6, whereas the expression of the nc-urf a gene completely restores the wild-type (non-mutator) phenotype. The significant similarity of the urf a gene to the mitochondrial var1 gene of S. cerevisiae and homologous genes in other yeasts suggests that the urf a gene product might be a ribosomal protein with a dual function in protein synthesis and maintenance of mitochondrial DNA integrity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050746
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