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  • 1
    Electronic Resource
    Electronic Resource
    Allelic variation of the D-prolamin subunits encoded at the Hch genome in a collection of primary hexaploid tritordeums (1999)
    Springer
    Theoretical and applied genetics 99 (1999), S. 296-299 
    Details
    ISSN: 1432-2242
    Keywords: Keys words Hordeum chilense ; Prolamins ; Tritordeum ; SDS-PAGE ; Genetic variability ; Bread-making quality ; Storage proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Hexaploid tritordeum is the amphiploid derived from the cross between Hordeum chilense and durum wheat. The storage proteins synthesised by the Hch genome have an influence on the gluten strength of this amphiploid. The D-prolamins of H. chilense are glutenin-like proteins. The variability has been analysed electrophoretically and up to 20 different patterns have been detected in a world collection of this species. This genetic variability of H. chilense could be a source of additional variation in tritordeum and in breeding wheat for quality.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001220051235
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  • 2
    Electronic Resource
    Electronic Resource
    Development and characterization of Hordeum chilense chromosome-specific STS markers suitable for wheat introgression and marker-assisted selection (1999)
    Springer
    Theoretical and applied genetics 98 (1999), S. 721-727 
    Details
    ISSN: 1432-2242
    Keywords: Key words Addition lines ; Multiplexed PCR ; RAPD ; Sequence tagged site ; Tritordeum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  RAPD markers were developed for octoploid×Tritordeum (amphiploid Hordeum chilense×Triticum aestivum) and its parents. Addition lines were used to identify specific RAPD markers for the Hordeum chilense chromosomes detectable in a wheat background. Twelve RAPD fragments have been cloned, sequenced and converted into STS markers. Eleven of these STSs have maintained both the chromosome specificity and the possibility of detection in a wheat background. The use of these markers in multiplexed PCRs facilitates both the efficient and reliable screening of new addition lines as well as the monitoring of introgression of H. chilense in bread and durum wheat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001220051126
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  • 3
    Electronic Resource
    Electronic Resource
    Chromosomal location in H. chilense and expression of common bunt resistance in wheat addition lines (1999)
    Springer
    Euphytica 109 (1999), S. 157-159 
    Details
    ISSN: 1573-5060
    Keywords: common bunt ; disease resistance ; Hordeum chilense ; Tilletia caries ; Tilletia tritici ; Tritordeum ; wheat additionlines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Hordeum chilense is resistant to common bunt. Addition lines of H. chilense in wheat were utilized in field experiments to determine which H. chilense chromosomes carry resistance genes. Resistance is conferred by gene(s) on chromosome 7 and to a minor extent by such on chromosome 6 of H. chilense. Expression of resistance was quantitative.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1003796807036
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  • 4
    Electronic Resource
    Electronic Resource
    Chromosomal location of resistance to Septoria tritici in Hordeum chilense determined by the study of chromosomal addition and substitution lines in `Chinese Spring' wheat (2000)
    Springer
    Euphytica 115 (2000), S. 221-224 
    Details
    ISSN: 1573-5060
    Keywords: Septoria tritici ; disease resistance ; Hordeum chilense ; Tritordeum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Hordeum chilense exhibits resistance to Septoria tritici. Addition and substitution lines of H. chilensein wheat were utilized in growth chamber and field experiments to determine which H. chilense chromosomes carry resistance genes. Resistance is conferred by gene(s) on chromosome 4 and, to a minor extent, by genes on chromosomes 5, 6 and 7.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1004097830103
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  • 5
    Electronic Resource
    Electronic Resource
    Acetylated and detyrosinated α-tubulins are co-localized in stable microtubules in rat meningeal fibroblasts (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 284-291 
    Details
    ISSN: 0886-1544
    Keywords: tyrosination ; acetylation ; post-translational modifications ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have examined the distribution of acetylated α-tubulin using immunofluorescence microscopy in fibroblastic cells of rat brain meaninges. Meningeal fibroblasts showed heterogenous staining patterns with a monoclonal antibody against acetylated α-tubulin ranging from staining of primary cilia or microtubule-organising centers (MTOCs) alone to extensive microtubule networks. Staining with a broad spectrum anti-α-tubulin monoclonal indicated that all cells possessed cytoplasmic microtubule networks. From double-labeling experiments using an antibody against acetylated α-tubulin (6-11B-1) and antibodies against either tyrosinated or detyrosinated α-tubulin, it was found that acetylated α-tubulin and tyrosinated α-tubulin were often segregated to different microtubules. The microtubules containing acetylated but not tyrosinated α-tubulin were cold stable. Therefore, it appeared that in general meningeal cells possessed two subset of microtubules: One subset contained detyrosinated and acetylated α-tubulin and was cold stable, and the other contained tyrosinated α-tubulin and was cold labile. These results are consistent with the idea that acetylation and detyrosination of α-tubulin are involved in the specification of stable microtubules.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970080309
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  • 6
    Electronic Resource
    Electronic Resource
    Regulation and evolution of the single alpha-tubulin gene of the ciliate Tetrahymena thermophila (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 27 (1994), S. 272-283 
    Details
    ISSN: 0886-1544
    Keywords: cell cycle ; transcription ; mRNA decay ; autoregulation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The single alpha-tubulin gene of Tetrahymena thermophila was isolated from a genomic library and shown to encode a single protein. Comparisons of the rates of evolution of this gene with other alpha-tubulin sequences revealed that it belongs to a group of more evolutionarily constrained alpha-tubulin proteins in animals, plants, and protozoans versus the group of more rapidly evolving fungal and variant animal alpha-tubulins. The single alpha-tubulin of Tetrahymena must be used in a variety of microtubule structures, and we suggest that equivalently conserved alpha-tubulins in other organisms are evolutionarily constrained because they, too, are multifunctional. Reduced constraints on fungal tubulins are consistent with their simpler microtubule systems. The animal variant alpha-tubulins may also have diverged because of fewer functional requirements or they could be examples of specialized tubulins. To analyze the role of tubulin gene expression in regulation of the complex microtubule system of Tetrahymena, alpha-tubulin mRNA amounts were examined in a number of cell states. Message levels increased in growing versus starved cells and also during early stages of conjugation. These changes were correlated with increases in transcription rates. Additionally, alpha-tubulin mRNA levels oscillate in a cell cycle dependent fashion caused by changes in both transcription and decay rates. Therefore, as in other organisms, Tetrahymena adjusts alpha-tubulin message amounts via message decay. However the complex control of alpha-tubulin mRNA during the Tetrahymena life cycle involves regulation of both decay and transcription rates. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970270308
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  • 7
    Electronic Resource
    Electronic Resource
    Colocalisation of acetylated microtubules, glial filaments, and mitochondria in astrocytes in vitro (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 10 (1988), S. 438-449 
    Details
    ISSN: 0886-1544
    Keywords: tyrosinated microtubules ; organelle distribution/transport ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have recently shown that acetylated α-tubulin containing microtubules (acety1-MTs; labeled by antibody 6-11B-1) constitute a cold-stable subset of the microtubule network of nonneuronal cells in rat primary forebrain cultures [Cambray-Deakin and Burgoyne: Cell Motil. 8(3):284-291, 1987b]. In contrast, tyrosinated α-tubulin containing MTs (tyr-MTs; labeled by antibody YL1/2) are cold-labile. Here we have examined the distribution of acety1-MTs and tyr-MTs in cultures of newborn rat forebrain astrocytes and simultaneously investigated the distribution of mitochondria and glial filaments. In double-label immunofluorescence experiments a marked colocalisation of acetyl-MTs and glial filament bundles was observed. Tyr-MTs did not show a similar colocalisation with glial filament bundles. Furthermore, the distribution of mitochondria closely followed that of the acetyl-MT and glial filament bundles. When cells were exposed to short-term (30-min) treatments with MT-disrupting agents such as colchicine and nocodazole, the tyr-MT network was removed but the distributions of acetyl-MTs, glial filaments, and mitochondria were unchanged. Increased exposure to colchicine (9-16 hr) caused a progressive disruption of the acetyl-MTs and the collapse of glial filaments and mitochondria to the perinuclear region. These results suggest that acetyl-MTs and glial filaments but not tyr-MTs may be involved in the intracellular transport of organelles and/or in the control of their cytoplasmic distribution.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970100311
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  • 8
    Electronic Resource
    Electronic Resource
    Perspectives on tubulin isotype function and evolution based on the observation that Tetrahymena thermophila microtubules contain a single α- and β-tubulin (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 25 (1993), S. 243-253 
    Details
    ISSN: 0886-1544
    Keywords: multitubulin hypothesis ; neighbor-joining method ; ciliate ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have cloned and sequenced the two β-tubulin genes of the ciliated protozoan Tetrahymena thermophila. The two genes encode identical 443 amino acid peptides which are 99.7% identical to the β-tubulin proteins of T. pyriformis and 95% identical to human β1 tubulin. T. thermophila contains only one β-tubulin gene (Callahan et al., 1984: Cell 36:441-445). Thus, all of the extremely diverse microtubule structures in this unicellular organism can be formed from a single α- and a single β-tubulin peptide. We have also carried out a phylogenetic analysis of 84 complete β-tubulin peptide sequences. This analysis supports two hypotheses regarding β-tubulin evolution and function: (1) Multifunctional β-tubulins are under greater evolutionary constraint than β-tubulins present in specialized cells or in cells with very few microtubule related functions, which can evolve rapidly; and (2) Cells which form axonemes maintain a homogeneous population of tubulins. © 1993 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970250305
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  • 9
    Electronic Resource
    Electronic Resource
    Developmentally regulated expression during gametogenesis of the murine gene meg1 suggests a role in meiosis (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 38 (1994), S. 16-23 
    Details
    ISSN: 1040-452X
    Keywords: Mammalian germ cell differentiation ; Gene expression ; Meiosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Previous studies have shown that in adult male mice, expression of the meg1 gene is restricted to meiotic and early postmeiotic testicular germ cells. We have now analyzed the expression of meg1 during postnatal testicular development and the comparable meiotic stages in the female. The 0.75 kb transcript for meg1 begins to accumulate in testes at d8-9 of postnatal (pn) development, coincident with the entry of germ cells into meiosis, and is expressed most abundantly at pn d14 and subsequent stages, when the spermatocytes have entered pachytene. In situ hybridization analysis shows that meg1 is expressed at very low levels in leptotene cells and increases as the cells progress through zygotene and pachytene stages. In the embryonic ovary, meg1 is not detected until after day 15 of gestation when the cells have entered the pachytene stage of meiosis I. In situ hybridization analysis suggests that meg1 transcripts are expressed at higher levels in degenerating rather than in healthy pachytene stage oocytes; meg1 is not expressed in any cells of the adult ovary, regardless of the stage of follicular development. These results suggest that meg1 is indeed a meiosis-associated gene in both male and female germ cells through the pachytene stage of meiosis I and appears to exhibit sex-specific differences in its expression thereafter. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080380104
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  • 10
    Electronic Resource
    Electronic Resource
    Male accessory sex glands produce heparin-binding proteins that bind to cauda epididymal spermatozoa and are testosterone dependent (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 25 (1990), S. 237-246 
    Details
    ISSN: 1040-452X
    Keywords: Seminal vesicle ; Prostate ; Bulbourethral gland ; Seminal plasma ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Heparin binds to bovine sperm and stimulates capacitation in vitro. Seminal plasma alters the ability of epididymal sperm to bind heparin, and several heparin-binding proteins (HBPs) have been identified in bull seminal plasma. This study had three objectives: (1) to identify production sites of seminal plasma HBPs, (2) to determine which HBPs bound to cauda epididymal sperm, and (3) to determine whether presence of HBPs was testosterone dependent. Proteins from bull or rat seminal vesicles, prostates, and bulbourethral glands were separated by heparin affinity high-performance liquid chromatography. HBPs were found in all accessory glands of rats and bulls, but the major source of bovine seminal plasma HBPs appeared to be seminal vesicles. Between 25% and 50% of the protein from each gland bound to the heparin column, and NaCl concentrations required to elute proteins ranged from 0.15 to 1.4 M. One-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that major HBPs were relatively small, with molecular weights between 13 and 31 kDa, but some HBPs also exhibited higher molecular weights, between 40 and 100 kDa. Radioiodinated HBPs from each bovine gland were incubated with epididymal sperm. Labeled HBPs binding to sperm exhibited molecular weights of 14, 16, 24, and 30 kDa as determined by SDS-PAGE and autoradiography. The HBP content of the accessory sex glands decreased significantly in castrated rats and was restored to levels of sham-operated controls by testosterone replacement. Heparin-binding proteins may play a role in fertilization by attaching to sperm surfaces, enabling heparin-like glycosaminoglycans in the female reproductive tract to induce capacitation.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080250305
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