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  • Life and Medical Sciences  (2)
  • B-chromosome
  • MAN/SYSTEM TECHNOLOGY AND LIFE SUPPORT
  • Polymer and Materials Science
  • 1995-1999  (4)
  • 1940-1944
  • 1998  (2)
  • 1996  (2)
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Publisher
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  • 1995-1999  (4)
  • 1940-1944
Year
  • 1
    ISSN: 1573-6849
    Keywords: B-chromosome ; DNA sequence composition ; PREM-1 element ; random amplification of polymorphic DNA ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The overall composition of the maize B is similar to that of the standard chromosome complement (A-chromosomes). This has been demonstrated by the use of several methods including: (a) genomicin situ hybridization (GISH), (b) analysis of highly repetitive sequences by the comparison of restriction digests of 0B and +B DNA and (c) the characterization of middle-repetitive cloned sequences. By the use of the technique of random amplification of polymorphic DNA-polymerase chain reaction, we have identified a B-specific repetitive sequence family. Sequence analysis of the B-specific clone reveals a relationship to the PREM-1 family of maize retroelements, which are preferentially transcribed in pollen. These results suggest an internal origin of the B-chromosome from within the maize genome, but demonstrate also that specific sequences can evolve by rapid processes of genomic turnover. Models for the origin of the maize B are discussed in the context of the present data.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1057-9257
    Keywords: gallium nitride ; nanocrystallites ; detonation ; gallium azide ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: High quality nanoscale, phase-pure hexagonal gallium nitride (GaN) crystallites have been synthesized by the thermal induced detonation of molecular precursors of the type (R3N)Ga(N3)3 (R=CH3, C2H5, etc.). The method allows the control of the particle size regime from 2 to about 1000 nm. X-ray diffraction and Rietveld simulations revealed an anisotropic platelet-like shape of the particles. The obtained GaN material was as well characterized by transmission electron microscopy and electron diffraction, photoluminescence spectroscopy, SEM, IR, RAMAN, thermal gas effusion/mass spectrometry, thermal analysis, elemental analysis. Gas absorption measurements (BET method) showed a specific surface area of about 90 m2 · g-1. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 869-875 
    ISSN: 0749-503X
    Keywords: calmodulin ; CMD1 ; ALG1 ; K. lactis ; EF hand ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The KlCMD1 gene was isolated from a Kluyveromyces lactis genomic library as a suppressor of the Saccharomyces cerevisiae temperature-sensitive mutant spc110-124, an allele previously shown to be suppressed by elevated copy number of the S. cerevisiae calmodulin gene CMD1. The KlCMD1 gene encodes a polypeptide which is 95% identical to S. cerevisiae calmodulin and 55% identical to calmodulin from Schizosaccharomyces pombe.Complementation of a S. cerevisiae cmd1 deletion mutant by KlCMD1 demonstrates that this gene encodes a functional calmodulin homologue. Multiple sequence alignment of calmodulins from yeast and multicellular eukaryotes shows that the K. lactis and S. cerevisiae calmodulins are considerably more closely related to each other than to other calmodulins, most of which have four functional Ca2+-binding EF hand domains. Thus like its S. cerevisiae counterpart Cmd1p, the KlCMD1 product is predicted to form only three Ca2+-binding motifs. The KlCMD1 sequence has been assigned Accession Number AJ002021 in the EMBL/GenBank database. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 3 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1647-1675 
    ISSN: 0749-503X
    Keywords: yeast ; phosphorylation ; protein phosphatase ; PP1 ; PP2A ; PP2B ; calcineurin ; Sit4 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Since the isolation of the first yeast protein phosphatase genes in 1989, much progress has been made in understanding this important group of proteins. Yeast contain genes encoding all the major types of protein phosphatase found in higher eukaryotes and the ability to use powerful genetic approaches will complement the wealth of biochemical information available from other systems. This review will summarize recent progress in understanding the structure, function and regulation of the PPP family of protein serine-threonine phosphatases, concentrating on the budding yeast Saccharomyces cerevisiae.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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