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  • isozymes  (2)
  • Amino Acyl-tRNA Synthetases/chemistry  (1)
  • 1995-1999  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Characterization of two morphological groups of isolates ofPythium ultimum var.ultimum in a vegetable field (1998)
    Springer
    Mycoscience 39 (1998), S. 135-144 
    Details
    ISSN: 1618-2545
    Keywords: intraspecific group ; isozymes ; morphology ; Pythium ultimum var.ultimum ; RAPD
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Comparisons were made between two morphological groups ofPythium ultimum var.ultimum strains isolated in a vegetable field in Japan. The groups were distinguished as having smaller or larger sexual organs by the sizes of their antheridia and oogonia. Morphological study indicated that the two groups comprised a single taxon,P. ultimum var.ultimum, by the current taxonomical keys. The smaller group grew faster in the lower temperature range of 4–15°C, whereas the larger group grew faster in the higher temperature range of 25–37°C. Random amplified polymorphic DNA (RAPD) and isozyme analyses revealed genetic dissimilarity between the two groups. Cluster analysis of the isozyme banding patterns with four otherPythium spp. demonstrated that the genetic dissimilarity between the two groups was equivalent to species level. In the field survey, the smaller group was frequently detected in February, May and September but not in July, while the larger group was detected mainly in July and September. The two groups were not distinguishable by their pathogenicity to spinach seedlings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02464051
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Classification ofPythium ‘group F’ based on mycelial protein and isozyme patterns (1995)
    Springer
    Mycoscience 36 (1995), S. 45-49 
    Details
    ISSN: 1618-2545
    Keywords: electrophoresis ; isozymes ; mycelial protein ; Pythium ‘group F’
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Taxonomic characteristics were compared among 10 isolates ofPythium ‘group F’ in tems of the electrophoretic patterns of their mycelial proteins and isozymes. These isolates were obtained from water of three ponds in different seasons and have an identical morphology of zoosporangia. Attempts to cross the isolates with each other themselves and with other isolates from the same group failed.Pythium ‘group F’ is the most dominant of the pythia in the aquatic ecosystem and is difficult to identify because of the lack of sexual reproductive structures. Isozyme analysis proved useful in this respect. Comparisons of banding patterns of total soluble proteins and isozymes revealed five subgroups inPythium ‘group F’. Two isolates obtained from water of different ponds in different seasons showed the same protein and isozyme patterns. Our findings indicate that the use of total soluble protein and isozyme patterns for determining the variation withinPythium ‘group F’ could become a valuable adjunct to the morphological and physiological criteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02268572
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    Paper (German National Licenses)
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  • 3
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    Architectures of class-defining and specific domains of glutamyl-tRNA synthetase (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-31
    Description: The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution. The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain. These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific recognition of the D and acceptor stems of tRNA(Glu) as indicated by mutagenesis analyses based on the docking properties of GluRS and tRNA. In striking contrast to the beta-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-alpha-helix architecture, an alpha-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nureki, O -- Vassylyev, D G -- Katayanagi, K -- Shimizu, T -- Sekine, S -- Kigawa, T -- Miyazawa, T -- Yokoyama, S -- Morikawa, K -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1958-65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biochemistry, School of Science, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701318" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acyl-tRNA Synthetases/chemistry ; Anticodon ; Biological Evolution ; Computer Graphics ; Crystallography, X-Ray ; Escherichia coli/enzymology ; Glutamate-tRNA Ligase/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Transfer, Glu/chemistry/metabolism ; Sequence Alignment ; Thermus thermophilus/*enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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