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  • Insertion sequence  (1)
  • Key words:Myo-Inositol methyl transferase  (1)
  • 2020-2020
  • 1995-1999  (2)
  • 1999  (2)
Collection
Publisher
Years
  • 2020-2020
  • 1995-1999  (2)
Year
  • 1999  (2)
  • 1
    ISSN: 1432-072X
    Keywords: Key words IS1389 ; Insertion sequence ; IS3 family ; XamI restriction-modification system ; Xanthomonas campestris pv. amaranthicola
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract IS1389, a new insertion sequence belonging to the IS3 family, has been identified in Xanthomonas campestris pv. amaranthicola. The genome of this bacterium contains at least 11 copies of the element, whereas no hybridizing sequences were detected in other Xanthomonas species [X. axonopodis, X. fragaridae, X. phaseoli, and X. (Stenotrophomonas) maltophila]. Two nearly identical copies of the element (IS1389-A and IS1389-B) were characterized. According to analysis of sequence alignments and similar structural features, IS1389 belongs to the IS407 subgroup of the IS3 family, which duplicates 4 bp of target DNA upon insertion. IS1389-A was found in the proximity of the modification gene of the XamI restriction-modification system.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Key words:Myo-Inositol methyl transferase ; Mesem-bryanthemum (salt stress) ; Plasma-membrane H+-ATPase ; Pinitol ; Salt tolerance ; Vacuolar H+-ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. A salt-tolerant stable cell-suspension culture from the halophyte Mesembryanthemum crystallinum L. has been established from calli generated from leaves of 6-week-old well-watered plants. Optimal cell growth was observed in the presence of 200 mM NaCl, and within 7 d cells were able to concentrate Na+ to levels exceeding those in the growth medium. Accumulation of Na+ was paralled by increases in the compatible solute pinitol and myo-inositol methyl transferase (IMT), a key enzyme in pinitol biosynthesis. Increasing concentrations of NaCl stimulated the activities of tonoplast and plasma-membrane H+-ATPases. Immunodetection of the ATPases showed that the increased activity was not due to changes in protein amount that could be attributed to treatment conditions. A specific role for these mechanisms in salt-adaptation is supported by the inability of mannitol-induced water stress to elicit the same responses, and the absence of enzyme activity and protein expression associated with Crassulacean acid metabolism in the cells. Results demonstrate that these  M. crystallinum cell suspensions show a halophytic growth response, comparable to that of the whole plant, and thus provide a valuable tool for studying signaling and biochemical pathways involved in salt recognition and response.
    Type of Medium: Electronic Resource
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